ID A0A099CYY1_9GAMM Unreviewed; 680 AA.
AC A0A099CYY1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=HNQ86_002104 {ECO:0000313|EMBL:MBB6184759.1}, LF63_0100680
GN {ECO:0000313|EMBL:KGI79188.1};
OS Oleiagrimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Oleiagrimonas.
OX NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI79188.1, ECO:0000313|Proteomes:UP000029708};
RN [1] {ECO:0000313|EMBL:KGI79188.1, ECO:0000313|Proteomes:UP000029708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.5X {ECO:0000313|EMBL:KGI79188.1,
RC ECO:0000313|Proteomes:UP000029708};
RA Fang T., Wang H.;
RT "Xanthomonadaceae 3.5X direct submission.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6184759.1, ECO:0000313|Proteomes:UP000560000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 107085 {ECO:0000313|EMBL:MBB6184759.1,
RC ECO:0000313|Proteomes:UP000560000};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:KGI79188.1}.
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DR EMBL; JROI01000002; KGI79188.1; -; Genomic_DNA.
DR EMBL; JACHET010000001; MBB6184759.1; -; Genomic_DNA.
DR RefSeq; WP_043098949.1; NZ_KN196470.1.
DR AlphaFoldDB; A0A099CYY1; -.
DR STRING; 1543381.LF63_0100680; -.
DR MEROPS; M03.004; -.
DR HOGENOM; CLU_001805_4_1_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000029708; Unassembled WGS sequence.
DR Proteomes; UP000560000; 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; 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; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 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:UP000029708};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 31..149
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 223..677
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 680 AA; 76004 MW; B1147B7C9CA3E0C4 CRC64;
MTTANPLLAD AALPAFDAIR PEHVLPAVEA VLADYRGAIA AMTAEGARHD FARVMLAQER
LEQRLNTVWS PVSHLHSVAD SKPLREAYDA ALEKITDFSA ELGQNRALYA AVKAVADAEG
DALPADRRAL IEHSLRDFRL SGVALEEPAR SRYRAIANEL SKLGTAFANA VLDATDAWQH
HITDERDLAG IPASGRAVLR QYAKEQDLDG YLVTLKQPAV QAVMTYADDR KLREKVYWAY
QTRASDQGPD AGTYDNSERI ERLLALRHEA AQLLGFANAA EESLATKMAE STQTVLDFLA
DLAARAKPVA RKELDTLRAF AAEHLDLANL EPWDTGYAAE KLRQQRYALD EEQIKPYFPL
PSVIDGLFAV TQRLYGIALK PREDVATWHP DARYYDVLDA DGRVFAGVYM DLYARSGKRG
GAWMDVCRSR FRDGETLQLP VAYLTCNFAP PTEDAPALLT HDDVLTLFHE FGHGLHHLLT
EVDLPSIGGI DGVEWDAVEL PSQFMENFAW NRDALDLFAR HYQTGERLPD DLFQRMLDAR
HFHAGLFLVR QLEFGLFDFH LHLDYDPERG ARTMAVLEQV RRQVAVLHPP AWQRFPHAFT
HIFAGGYAAG YYSYLWAEVL SADAFERFEQ AGVIDRETGE AFRREILSVG ATRPALESFV
AFRGRAPEPA ALLRSYGLAA
//
