ID D2TTM0_CITRI Unreviewed; 252 AA.
AC D2TTM0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:CBG91723.1};
GN OrderedLocusNames=ROD_50501 {ECO:0000313|EMBL:CBG91723.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91723.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91723.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91723.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG91723.1; -; Genomic_DNA.
DR RefSeq; WP_012908865.1; NC_013716.1.
DR AlphaFoldDB; D2TTM0; -.
DR STRING; 637910.ROD_50501; -.
DR MEROPS; M48.022; -.
DR KEGG; cro:ROD_50501; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_074068_0_0_6; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000001889; Chromosome.
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:SF4; METALLOPROTEASE LOIP; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..252
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003036688"
FT DOMAIN 72..245
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 223..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 26645 MW; 83EBC2F9791E7420 CRC64;
MKIRALLLAM GMASVLTGCQ NMDSNGLLSS GAEAFQAYSL SDAQVKALSD QACAEMDGKA
TIAPAGSEYA KRLNTIAAAL GDNINGQAVN YKVYMAKDVN AFAMANGCIR VYSGLMDMMT
DNEVEAVIGH EMGHVALGHV KKGMQVALGT NAVRAAAASA GGIVGSLSQS QLGDLGEKLV
NSQFSQRQES EADDYSYDLL RKRGISPAGL ATSFEKLAKL EEGRQSSMFD DHPASAERAQ
HIRDRMKADG IK
//
