ID A7MKM7_CROS8 Unreviewed; 695 AA.
AC A7MKM7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN OrderedLocusNames=ESA_04224 {ECO:0000313|EMBL:ABU79404.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU79404.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU79404.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU79404.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC Ala commonly occur as P1 or P1' residues, but more distant residues
CC are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC Evidence={ECO:0000256|ARBA:ARBA00024603};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP000783; ABU79404.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MKM7; -.
DR SMR; A7MKM7; -.
DR MEROPS; M03.004; -.
DR KEGG; esa:ESA_04224; -.
DR HOGENOM; CLU_001805_4_1_6; -.
DR Proteomes; UP000000260; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF19310; TOP_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000000260};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 46..163
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 237..692
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 695 AA; 78606 MW; 0E799E9FD56A7DDE CRC64;
MSLQDALNNT NQDALMTNPL LTPFELPPFS SIKPEHVVPA VTKALEDCRA QVEAIVGRGA
PYSWESLCQP LAETDDRLGR IFSPISHLNS VKNSPELREA YEQTLPLLSE YSTWVGQHEG
LYQAYRDLRD GENYAKLDTA QKKAVDNALR DFELSGIGLP KEKQKRYGEI AARLSELGSL
YSNNVLDATQ GWTKLITDES ELSGMPESAQ AAAKAMAEAK EQEGFLLTLD IPSYLPVMTY
CDNQALREEM YRAYSTRASD QGPNAGKWDN TPVMEEILAL RHELAQLLGF DSYADKSLAT
KMAENPQQVL DFLTDLAKRA RPQGEKELAQ LRAFAKEHFS VDELQPWDIA YYSEKQKQHL
YSISDEQLRP YFPENKAVNG LFEVVKRIYG ISAKERKDID VWHPDVRFFE LYDESGELRG
SFYLDLYARE NKRGGAWMDD CVGQMRKADG SLQKPVAYLT CNFNRPVSGK PALFTHDEVI
TLFHEFGHGL HHMLTRIETP GVAGISGVPW DAVELPSQFM ENWCWEPEAL AFISGHYETG
EPLPQELLDK MLAAKNYQAA MFILRQLEFG LFDFRLHAQF SPEQGAKVLE TLAEIKKQVA
VVPGPSWGRF PHAFSHIFAG GYAAGYYSYL WADVLAADAY SRFEEEGIFN RETGQSFLDN
ILTRGGSEEP MELFKRFRGR EPQLDAMLEH YGIQG
//
