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Database: UniProt
Entry: A0A061P436_9BACL
LinkDB: A0A061P436_9BACL
Original site: A0A061P436_9BACL 
ID   A0A061P436_9BACL        Unreviewed;       598 AA.
AC   A0A061P436;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=JCM19039_722 {ECO:0000313|EMBL:GAK11049.1};
OS   Geomicrobium sp. JCM 19039.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX   NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK11049.1, ECO:0000313|Proteomes:UP000027177};
RN   [1] {ECO:0000313|EMBL:GAK11049.1, ECO:0000313|Proteomes:UP000027177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK11049.1,
RC   ECO:0000313|Proteomes:UP000027177};
RA   Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA   Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT   JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL   Genome Announc. 2:e00622-14(2014).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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:GAK11049.1}.
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DR   EMBL; BAXB01000002; GAK11049.1; -; Genomic_DNA.
DR   RefSeq; WP_042423812.1; NZ_BAXB01000002.1.
DR   AlphaFoldDB; A0A061P436; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000027177; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
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; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027177};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          115..183
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..584
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   598 AA;  68994 MW;  B4AC5BF070FC7D6C CRC64;
     MATSYTSRED VPEQEKWDLT DLYENEEAWQ KDVDTCKQLA DELAQFEDNI TDASSLLAYL
     KKQEHLSLIA RKVFAYSMFL SDIDTRDTNA QRLSGKAAQL SVKMSEASAF FMPFLLSLSK
     DTLTSYINEE KELQYFEDEL WKSFRYKPHV LSKEQEELLS QLSETIGAPS NTYNMYNNAD
     IQFGMVHNEE GEEVQLTRGM YSKMLEDEDR DVRKAAYKAY YKPYLQMNNT IATNYASEVK
     TNASLAKIRN YNSALDEALF SDNIPSEVYE NLLQAAKDNS QPLHDYAKLR KERLAVQELR
     QYDLSAPIVA GVKEDIPYDE AYETMIQALM PLGDDYIEQL RAFKDKRNID VRETKGKKSG
     AYNMGVYGVH PFVLLNHNDD LNSLFTLVHE MGHALHSHYS SKMQPQISAS YKIFVAEVAS
     TVNEVLLIQH LLKETTDQKK RAYLLNHFIE QFRGTFFTQV MFADFEKQTH ERAEAEEPLD
     ASSLNELYEG LFRTYFGDEI VFDDEVKYGW SRIPHFYRAF YVYQYATGFV SAIDIAMRIL
     DGDEETLKNY HTFLQSGSVK DPLDLLLDTG VDLTSDVPIK NALNMFKNTV DELRKLDV
//
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