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Database: UniProt
Entry: A0A1T5PC57_9BACT
LinkDB: A0A1T5PC57_9BACT
Original site: A0A1T5PC57_9BACT 
ID   A0A1T5PC57_9BACT        Unreviewed;       268 AA.
AC   A0A1T5PC57;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Putative metalloprotease {ECO:0000313|EMBL:SKD09968.1};
GN   ORFNames=SAMN05660461_5868 {ECO:0000313|EMBL:SKD09968.1};
OS   Chitinophaga ginsengisegetis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD09968.1, ECO:0000313|Proteomes:UP000190166};
RN   [1] {ECO:0000313|EMBL:SKD09968.1, ECO:0000313|Proteomes:UP000190166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD09968.1,
RC   ECO:0000313|Proteomes:UP000190166};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; FUZZ01000006; SKD09968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5PC57; -.
DR   STRING; 393003.SAMN05660461_5868; -.
DR   Proteomes; UP000190166; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07334; M48C_loiP_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   PANTHER; PTHR22726:SF8; METALLOPROTEASE YCAL; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..268
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012233883"
FT   DOMAIN          93..253
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          224..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   268 AA;  29123 MW;  86B9F750C0BA59E9 CRC64;
     MSVYARFGFV CALTMSFALA SNAQLKLNAK TLGAGAKAVK AATLTDDDVI RYTKEYIQWM
     DEHNPVAPAD DPMAQRLKKL TDHVTSYEGM NLNFKVYLVR DINAFACADG SVRVCAGLLQ
     TMTDDEVMGV IGHEIGHVKN KDSKDAFKTA LMTSALKDGV SSQGGTAGTL SDSQLGELGE
     AVANSAYSRN QESQADNYGY EFLKAAKLNP WGMSMAFEKL WKASQESSGD KKKGSQLFSS
     HPDTEKRMNT MAEKAKKDGY EKPVVAAK
//
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