ID W4Q4Q7_9BACI Unreviewed; 590 AA.
AC W4Q4Q7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:GAE26349.1};
GN ORFNames=JCM9140_2401 {ECO:0000313|EMBL:GAE26349.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE26349.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE26349.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE26349.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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|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:GAE26349.1}.
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DR EMBL; BAUT01000023; GAE26349.1; -; Genomic_DNA.
DR AlphaFoldDB; W4Q4Q7; -.
DR STRING; 1236970.JCM9140_2401; -.
DR MEROPS; M03.A08; -.
DR Proteomes; UP000018890; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; 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 InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 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|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000018890};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 108..174
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 196..574
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 590 AA; 67505 MW; EEAACE932ECA7728 CRC64;
MNYPEVWDLD SIFRGGSESK EFKEFVIGND RQIDELNEAI GEEASFDQLE DYIHRIQIQM
QRNRQSSAFV SCLTAQNVKD KEASLWLGKM TEQSTKIQMI WGKIEDFLVE LTEEQWNEFS
KRPALKSVLF HLKERRFQAT EKLSPNEEKL AAKLEIDGYH AWGKVYNEAV GRMQIPFEEK
GVEKPLSAGQ LQNRLNSSDR SVRERAEIAS ERAWEKETDL FASTLNHLAG FRLQLYKARG
WDQVLKEPLA INRMQETTLT AMWETITDNK PRFYEFMARK AELLGVKKLA MHDVHAPLPV
EGDTNIPYSE ACELIIKHFK QISPKLAAFT EGALRDGWVE AEDRAGKRPG GFCTTFPLSK
ESRIFMTYDG TMANVATLAH ELGHAYHSHC LKDMAPLAQR YAMNVAETAS TFAENIIADA
LVKEAPTEEA TLSLLENKIS RSLAFFMNIH ARFLFETRFY EARKEGFVPV TQLNTLMEEA
QKEAYGGQLA TYSPTFWASK LHFHITGVPF YNFPYTFGFL FSLGIYKKAM ETGSSFEDDY
IALLQDTASM TVEDLAKKHL NVDLTSKSFW QEAIDVILKD VDTFMELTKS
//
