ID   A0A0M2H5R0_9MICO        Unreviewed;       637 AA.
AC   A0A0M2H5R0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:KJL39344.1};
DE            EC=3.4.24.70 {ECO:0000313|EMBL:KJL39344.1};
GN   Name=prlC {ECO:0000313|EMBL:KJL39344.1};
GN   ORFNames=RS81_01974 {ECO:0000313|EMBL:KJL39344.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL39344.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL39344.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL39344.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL39344.1}.
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DR   EMBL; JYIZ01000050; KJL39344.1; -; Genomic_DNA.
DR   RefSeq; WP_045275912.1; NZ_JYIZ01000050.1.
DR   AlphaFoldDB; A0A0M2H5R0; -.
DR   STRING; 92835.RS81_01974; -.
DR   PATRIC; fig|92835.4.peg.2001; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000033956; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06455; M3A_TOP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 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:UP000033956};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          210..631
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   637 AA;  71218 MW;  8E6417A37EDD28B4 CRC64;
     MTVALLTFPT DAAGWLTFAA ERPAERFDRV RAVDARLIAE TELSTRERLE LWNDADIALA
     EATSEAYLLS EAHPDAAVRE AAEQQVEKAE KLAADRLLDR ELWAVFADAD AAGLADDEQR
     LLEHLVRDFR RGGVDLDDEA RARVGELTER DTALSLAFSR NVREGRREIR VAPEALAGLP
     QDFIDAHPVG DDGLVALTTE YTDLMPVREY ARSRETRLAM LSAYNDLAWP ENDAVLAELL
     AVREERARLL GFTDWADYET GTRMIGSGAA IPRFLAQVDA ASAPASLPEY ERLLARLQED
     EPDAEEVTIA DFWYLLSRIK REQYDVDAQE VRSYFGFDQV LQGVLDVTGR LLDVEYRPVS
     PGTWHADVQS FEVFRGDDLL GRIHLDLHPR DGKFNHAACF PLVPGIAGRS FPEAVLLCNF
     SRGRLEHDEV VTFFHEFGHL VHDILGGRQR WSRFTGVATE WDFVEAPSQL LEEWAWDAGV
     LATFTANADG EPIPADLVAR MRTADAFGRA LEVRRQLGHA TVSYHLHVDR PADLQQATER
     LYASTSPVQP VRGLHSYAGF GHLTGYGACY YTYQWSLVIA RDLLSAFDGD LMDAAVAARY
     RELILEPGGS RDAADLVRSF LGRDYAFDAY AEWLEGA
//