CAZyme Information: MGYG000002338_00529

Basic Information

• Species: Staphylococcus haemolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus haemolyticus
• CAZyme ID: MGYG000002338_00529
• CAZy Family: GH23
• CAZyme Description: Chromosome partition protein Smc

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2070		227271.97	10.6208

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002338	2548117	Isolate	Russia	Europe

• Gene Location: Start: 44228; End: 50440 Strand: +

Full Sequence      

MADFNLGAEVSMDVDPLKASSKTLERQLKGINKSLREQRKEFKQNEMSAEQLANMEGDLG
RAIKAQEGLLARRKKALQDVKDEMAKSGKATDEQRIKLQQADGAYKKAQNQLNSYTKELK
DVQVASKTFGKTSDDIKGKLNSLRNEVKLNEAEFQKSSKATSDYEKHIDSLSASLTKSEN
AIKELEDNLKIVSDLKGENSREAKKLSSEIEKERLSYSQLEVTLSKVKNEFEDVKNENSE
LSQSIKTTEKFIDNMKDTANSLSNELKQSSASFKASSQETDDYKTHLQQLTNIQTKQKNV
INELEDEYKKVTAIQGTSSQQAKQLKSEIDKQRTAFTSLDAQINQATKQYDEYRLTNSQT
SITLGEAKRRLDSYNNALELNTVKFKSANKSVESYQTQLNHTNATITQHKTVLEGLERRY
EEVANTQGRNSVEADKVRNELYKEAIALQAAQNRADELSDELDKVARSQRKVRLATTLMG
AGFAGARDSADRIATTLRSVGEVTQGVVGEVMATQFTNLVPIMGSVVSAGAGVGGMVTAL
SGAAIGMGGSYAIALGAVKAFTGQATYALKMLEDGTLSITSETARYQQSLASLKTQWEGL
IAQNQAKIFNTMTNGINMAKTALSQLNPFLTTTAGQIERFSSRLLNWVNTSNNVKNAFNI
LNTQGTQAFGHLLNGAFHFVDGTVAVFNKLSPLFVWASKGFENMALSFRRWANSVEGSRA
INNFIEYTKTNLPIIGRIFGNIFGGIFNLFSAFSGHSHNVLLGIESVTEGFKNWSAELKR
SDGFQQFVQYLETNGPKVWTLIKNITGILWGLIKGMAPVGAVTLSVTNAITGWMSSMMNT
HPIIGQLIGSIVAGGGALLLFLKPLFLIKGALGGMRGALLAVTGAQKLFGATGAFATLGM
KRQTLQTKIATVATKTWALVTKGAALATKGLGLAIRFMTGPIGIAITVIGALVAGIIYLW
KNNETFRNFVINAWNAIKNTAISVFGFLKPYIINIWNAIKNGSIAIWNGMKAIASATWNG
IKFAIQNPIQALKMVITGIFTGIKNVSLAIWNALKTGVITIIRLWVSTSMATFRGLSTFF
SNLWNGIKSVAISAWNGIKNGVLTIIRLWIATSKATFNGLRSFFINLWNFIKNISIKTWN
TIKNGVLGAVRLLNTGVRKIFGTLRSWIISTWTSIKNKVVALAKLLYVGAKAAFNSLWNA
TKKIFTTLKNWALNNWRALKNGIVKLAKAIYTGVKNAFNSLWSSTKNIFNKLKNWAINTW
RSLKNSVVKLAKSLYSSVKNTFNNLWSSTKNIFSKLKNWLVNTWRSIKNKVTDLAKSLWN
GVKNTWSKMKSGTHNTMSKISSGTKSTWRGMKNSVVDISKALWSKVRGTFTNMRDGLKSI
IGKIKSHIGGMVNSVKNGLNKLIDGVNWVAGKLDMDKLPKIKLSTGTESTHTQNYVTNGK
LNQNTLATVGDKGKGNGPGGFRHETIIPPKGKPFITPAKDTTMPLSKGTRILNGAQTHAM
LSNGMTPMFNTGTIPRFASGTKKKLFQAVGETAGKFFNSAKKLKHNAMDSIGDKTKQAKE
WGSEKLSQIKDAVGKGTKWLSDKVGDIADWVGKPGKLLNKVLGAFGVNMDAFGIAKSAEI
PYNLMKAMFGKLKEAAKNLIDGWLEDEFSGGGGYNPYTKAPFHMTRGWTPSGHAGIDYGA
PTGTPIPSPIDGKVIQSWFSPNQPSGGNETQIWDGQKYTHIFMHQSKRKVKTGDRVHQGQ
IIGLVGNTGNSFGSHLHWQVNKGKGYLNNHPDSVNPLTWAKQAAKSGGGVNKAASAWKPD
IRRAAKAIGVRVSNADVNDVARLIQTESSGNAGVTQQIQDRNSGGNEAQGLLQYTPGSFS
SYAIRGHKNIKNGYDQLLAFFNNTDWRANLSYWKRRMASGLTGWGPTGSRKKYAKGTNSA
YRGLSTVFEEGGEIMNLRGGEQIIPNDVSIAAIESVINSDIFDRTQSAVYEAISRFADGL
REQKENKDNWIEQLYLKQVEENTELKNQNSILMQVVNKLDQLLNVNNQVAQTNEGILHKE
YFDSDKMSKKHNENMRKEAITKLMGKGGNV

Enzyme Prediction     

No EC number prediction in MGYG000002338_00529.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.91e-30	1671	1768	1	95	Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
cd12797	M23_peptidase	5.15e-29	1673	1760	1	85	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
COG5412	COG5412	1.13e-24	1072	1607	117	567	Phage-related protein [Mobilome: prophages, transposons].
cd13402	LT_TF-like	1.86e-23	1817	1947	1	113	lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
COG1196	Smc	8.00e-22	17	465	381	924	Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QXV71939.1	1.10e-317	409	2035	181	1795
AGW43750.1	6.16e-315	409	2064	181	1809
BAE05065.1	2.12e-314	1387	2065	830	1485
QXN77108.1	2.06e-304	1398	1947	1072	1614
AID01516.1	1.51e-276	409	2064	181	1741

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6V8I_AF	2.37e-76	493	978	249	734	ChainAF, Tape Measure Protein, gp57 [Dubowvirus dv80alpha],6V8I_BF Chain BF, Tape Measure Protein, gp57 [Dubowvirus dv80alpha],6V8I_CF Chain CF, Tape Measure Protein, gp57 [Dubowvirus dv80alpha]
5KQB_A	4.86e-13	1673	1763	29	118	Identificationand structural characterization of LytU [Staphylococcus aureus],5KQC_A Identification and structural characterization of LytU [Staphylococcus aureus]
6SMK_A	1.14e-12	1652	1779	2	129	Crystalstructure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_B Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_C Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_D Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_E Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583]
2HSI_A	9.00e-12	1659	1760	163	264	Crystalstructure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1],2HSI_B Crystal structure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1]
4QP5_A	1.75e-11	1643	1759	11	118	Catalyticdomain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QP5_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate [Staphylococcus simulans bv. staphylolyticus],4QPB_A Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans],4QPB_B Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the absence of phosphate [Staphylococcus simulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0PDK7	1.22e-31	569	858	159	447	Tail tape measure protein gp18 OS=Bacillus phage SPP1 OX=10724 PE=4 SV=1
O05156	1.97e-11	1632	1759	116	235	Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
P44693	8.40e-11	1659	1787	330	453	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
P0AFS9	9.73e-11	1673	1778	314	409	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT0	9.73e-11	1673	1778	314	409	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
808	830
843	862
877	899
937	959