CAZyme Information: MGYG000002415_00315

Basic Information

• Species: Proteus sp001722135
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus sp001722135
• CAZyme ID: MGYG000002415_00315
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1C

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
774		87157.93	9.4402

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002415	4051274	Isolate	not provided	not provided

• Gene Location: Start: 42737; End: 45061 Strand: +

Full Sequence      

MGGFLVILFCVGFRLFPHPALSEGFLSSTAYYDSNGNLLRLTLANDERYRLWTDLDDISP
LMINSAMRYEDRWFYYHAGFNPYSLIRGFFVSYIYGERLQGGSTITMQLARMHWQLNTRT
VGGKFIQVLRAIQLELSYSKHDILEAYFNYAPYGRNIESIGAASLIYFNKKPKELTLPEA
LTLAVLPQSPSYRIEPNSDGISLSLMKTRNQLYDYWLEEYPNDANLSALFQLPLRLRQPE
KMPYIAPHFIEQIEKQEKFNPRKPTNIVTTLDLPLQRLVEKQVDAFIERNKHLGVKNASV
ILVDTRDMGVKALIGSADYYNADIHGQVNGTNAKRSPGSTLKPFIYALGLEQGILHPRTI
LKDVPSTFGSYAPENFDLRFLGPISATQALNYSRNIPAVSIAAQLKNPTLYQFLQMSGIS
NMASERHYGLSLVLGGGEITVQELAKLYAILANRGKLKPLRMQSTDAIAKPIQLLSEEAS
FITLDMLSQHRRPGDTLAQKSTALPIYWKTGTSWGFRDAWSSGVFGPYVLIVWIGNFDGK
GNSALIGAEAAAPLFFNIIDNIIADYPNLKEPRFKLPENIKQVDVCLTSGNLPTPWCQRK
GKTWFIPGKSPIKVDTVYRPLAIDKATGEVVCPPYNEERVKIEVFEYWPSDLAKVFAQAG
LPKRTPPSTTHCKNGGSAILGMPPRILSPLRNTTYTLRRSSSPNTSIVFNATADNDSNII
YWFVDEAYLGSSTNQRSIEWYPKESGRYRIRAVDDKGRADTRNIRVDILGVINK

Enzyme Prediction     

No EC number prediction in MGYG000002415_00315.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	47	194	1.8e-43	0.8361581920903954

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02073	PBP_1c	0.0	18	766	1	726	penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG4953	PbpC	0.0	2	766	11	731	Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
PRK11240	PRK11240	3.99e-122	55	767	67	772	penicillin-binding protein 1C; Provisional
COG0744	MrcB	6.10e-115	28	594	55	628	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074	PBP_1a_fam	4.39e-99	49	555	1	521	penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPB80593.1	0.0	1	774	13	786
QQP26600.1	0.0	1	774	13	786
QIG05045.1	0.0	1	774	13	786
QPN91254.1	0.0	1	772	13	784
QIF95276.1	0.0	1	772	13	784

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FGZ_A	8.08e-33	31	573	137	704	E.coli PBP1b in complex with FPI-1465 [Escherichia coli K-12],5HL9_A E. coli PBP1b in complex with acyl-ampicillin and moenomycin [Escherichia coli K-12],5HLA_A E. coli PBP1b in complex with acyl-cephalexin and moenomycin [Escherichia coli K-12],5HLB_A E. coli PBP1b in complex with acyl-aztreonam and moenomycin [Escherichia coli K-12],5HLD_A E. coli PBP1b in complex with acyl-CENTA and moenomycin [Escherichia coli K-12],6YN0_A Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity [Escherichia coli K-12],7LQ6_A Chain A, Penicillin-binding protein 1B [Escherichia coli K-12]
3VMA_A	8.70e-33	31	573	158	725	CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]
3FWL_A	2.35e-30	50	573	160	708	CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli]
3UDF_A	4.65e-28	58	472	47	558	ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
2JE5_A	2.30e-26	56	593	60	665	StructuralAnd Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6],2JE5_B Structural And Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76577	1.18e-97	46	761	60	764	Penicillin-binding protein 1C OS=Escherichia coli (strain K12) OX=83333 GN=pbpC PE=1 SV=1
P70997	9.52e-47	28	614	54	656	Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
Q89AR2	8.94e-43	50	559	157	689	Penicillin-binding protein 1B OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=mrcB PE=3 SV=1
O66874	1.53e-41	3	580	18	683	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P38050	6.08e-41	4	584	21	614	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2

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
0.000241	0.999115	0.000164	0.000162	0.000149	0.000139

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002415_00315.