CAZyme Information: MGYG000002346_01227

Basic Information

• Species: Acinetobacter pittii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter pittii
• CAZyme ID: MGYG000002346_01227
• CAZy Family: CBM5
• CAZyme Description: Extracellular serine proteinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
393	MGYG000002346_13|CGC1	40979.96	7.383

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002346	3962855	Isolate	United States	North America

• Gene Location: Start: 76880; End: 78061 Strand: +

Full Sequence      

MKFCQVSTFLLAIALSHLTYAAPATTNSVLGSSEAKGIIKNQYIIILNKDVDSSKEFAQG
IAKQHGGKVLQTYDTVLKGFAIYLPNVADPAFVEAMKKNPKVVSVENDTIMKIDATTQSN
PDWGLDRIDQRNLPLDSAYSYLQTGSGTTAYIVDTGILSTHQQFSGRVLSGYTAISDGNG
TSDCHGHGTHVAGTVGGSTYGVAKNVSLVPIRILGCDGSGASSNVIAGLDWILKNGKKPA
VVNMSLGGDANTSLDSAVENLFNNGYVIVVAAGNSNTDACSTSPARVSKAITVAATDSTD
ARASYSNYGSCVDIFAPGSQINSSWIGSNTATKVLNGTSMATPHVVGVVAEMLQSTPTAT
PQTISNNLLNQASNNVVKNPSGSPNRLLYKSAQ

Enzyme Prediction     

No EC number prediction in MGYG000002346_01227.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04077	Peptidases_S8_PCSK9_ProteinaseK_like	1.26e-130	123	374	1	255	Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
cd07484	Peptidases_S8_Thermitase_like	6.05e-57	122	372	10	256	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
cd07477	Peptidases_S8_Subtilisin_subset	6.07e-57	152	368	6	226	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07487	Peptidases_S8_1	4.97e-56	145	372	1	263	Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07473	Peptidases_S8_Subtilisin_like	3.80e-49	170	370	48	256	Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOC24262.1	1.20e-104	39	389	21	378
QRK11067.1	1.93e-103	21	388	26	403
ADO75815.1	1.35e-98	39	389	47	398
CTQ90342.1	1.18e-92	38	387	40	387
AXO37891.1	2.90e-91	39	392	21	377

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WSL_A	8.61e-108	117	389	2	275	Structuralstudies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220],5WSL_B Structural studies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220],5WSL_C Structural studies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220]
4DZT_A	1.47e-105	117	389	2	273	AqualysinI: the crystal structure of a serine protease from an extreme thermophile, Thermus aquaticus YT-1 [Thermus aquaticus]
2B6N_A	4.03e-98	118	392	3	278	The1.8 A crystal structure of a Proteinase K like enzyme from a psychrotroph Serratia species [Serratia sp. GF96]
1S2N_A	1.98e-97	118	392	1	273	Crystalstructure of a cold adapted subtilisin-like serine proteinase [Vibrio sp. PA-44],1S2N_B Crystal structure of a cold adapted subtilisin-like serine proteinase [Vibrio sp. PA-44],1SH7_A Crystal structure of a cold adapted subtilisin-like serine proteinase [Vibrio sp. PA-44],1SH7_B Crystal structure of a cold adapted subtilisin-like serine proteinase [Vibrio sp. PA-44]
3F7M_A	1.40e-57	116	350	2	236	Crystalstructure of apo Cuticle-Degrading Protease (ver112) from Verticillium psalliotae [Lecanicillium psalliotae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P80146	2.20e-114	22	389	24	407	Extracellular serine proteinase OS=Thermus sp. (strain Rt41A) OX=32063 PE=1 SV=3
P08594	1.73e-108	39	389	51	400	Aqualysin-1 OS=Thermus aquaticus OX=271 GN=pstI PE=1 SV=2
P16588	4.42e-99	22	389	37	413	Alkaline serine exoprotease A OS=Vibrio alginolyticus OX=663 GN=proA PE=3 SV=1
L8FSM5	8.57e-77	1	389	1	395	Subtilisin-like protease 2 OS=Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) OX=658429 GN=SP2 PE=1 SV=1
A1CWF3	1.62e-74	77	389	85	399	Alkaline protease 1 OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=alp1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000209	0.999144	0.000149	0.000168	0.000155	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002346_01227.