ID A0A0F5ARM7_9GAMM Unreviewed; 680 AA.
AC A0A0F5ARM7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=WN56_08225 {ECO:0000313|EMBL:KKA44858.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA44858.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA44858.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA44858.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA44858.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAQR01000006; KKA44858.1; -; Genomic_DNA.
DR RefSeq; WP_046074582.1; NZ_LAQR01000006.1.
DR AlphaFoldDB; A0A0F5ARM7; -.
DR MEROPS; M03.004; -.
DR PATRIC; fig|1406902.3.peg.1679; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
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; 1.10.1370.40; -; 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:UP000033449};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 29..147
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 221..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 680 AA; 76837 MW; 4F2F0EB935CA6A39 CRC64;
MSNPLLQFED LPPFSAIKPE HVKPAVEAAI ADCRQAVDAA AATEQPSWDS VSVPVTEAED
RLGRIWSPVS HMNAVVNSQP LREAYESCLA LLSEYSTWRG QHKGLYQAYK AMKDSAEFSA
LDVAQQKAIN DALQDFELSG IALPADQQHR FGEIQKRLSE LSSSFSNNVL DATMGWSKLI
SDESDLAGLP ESARNAAKAQ AESKSQQGYL FTLDIPSYLP VMMYCDNRAL RQEMYEAFTT
RASDRGPQAG QWDNTELMNE SLRLKHELAR LLGFNHYSEL SLATKMAETP DQVMGFLNDL
VDKARPQGER EFAEVKAYAK EEFGVDALEP WDIPYYSEKL KQARYTISDE ALRPYFPEAR
VLSGLFEVMH RVFGMTITER KGIDTWHESV RFYDIHDSQG TLRGSFYLDL YARENKRGGA
WMDECRVRRR QADGELQTPV AYLTCNFNPP VGDDPALFTH DEVVTLFHEF GHGIHHMLTQ
VDVADVSGIN GVPWDAVELP SQFLENWCWE QEALSFISGH YQTGEALPED MLEKMLAAKN
FNSAMAMLRQ LEFSLFDFRL FSEFDPEVGP RIMETLSAVR EQVSVVPAPE WNRFPHAFGH
IFAGGYSAGY YSYKWAEVLS SDAYSRFEEE GIFNRDTGED FLNHILSRGG SEAPKDLFVR
FRGREPSPDA LLRHSGITTA
//
