ID W7CEV5_9LIST Unreviewed; 597 AA.
AC W7CEV5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EUJ35442.1};
GN ORFNames=BCAMP_11620 {ECO:0000313|EMBL:EUJ35442.1};
OS Brochothrix campestris FSL F6-1037.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ35442.1, ECO:0000313|Proteomes:UP000019243};
RN [1] {ECO:0000313|EMBL:EUJ35442.1, ECO:0000313|Proteomes:UP000019243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ35442.1,
RC ECO:0000313|Proteomes:UP000019243};
RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Novel taxa of Listeriaceae from agricultural environments in the United
RT States.";
RL Submitted (DEC-2012) 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|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:EUJ35442.1}.
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DR EMBL; AODH01000056; EUJ35442.1; -; Genomic_DNA.
DR RefSeq; WP_035315588.1; NZ_AODH01000056.1.
DR AlphaFoldDB; W7CEV5; -.
DR STRING; 1265861.BCAMP_11620; -.
DR MEROPS; M03.A08; -.
DR PATRIC; fig|1265861.3.peg.2279; -.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000019243; 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:UP000019243};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 115..179
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 201..579
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 597 AA; 67029 MW; 938D05E01B56F5CD CRC64;
MTTNYSLSWD IDTFFTGGSH SEAFQAKLDN TTKELHAFST AVSDWNGTDY NSFVTLIDTY
TTLRMALFQM SSFIECVAAA DASDTYSDTL LNKIGSLSAA LKNASNDLAQ QTLLLEDATW
EEWLTRTELH DVAFVLAELR SNQAHLLSAK EETLINNLSV DGYNAWAAHY DTLVGTMRFD
VVTETGEIAS LSAGQTDNLL NAADYKVRHD AFAVWQKTWQ EKAPLFADTL NHLIGFRLAK
YEARHWDVLD ESLRLNRLNE ATLTSIWTVV AQNKTPLLAF LKRKAALLGL DQLGWVDVEA
PLNLGATQTI RNFQTGADFI EENFAKFSPE MAAFAHNAFA NSWIEAEDRD NKRPGGFCIE
FPEDGESRIF MTYDGSANTI STLAHELGHA FHSHVMRDQS ALNRDYAMNV AETASTFAEI
LISDAAIKAA TSKAEKIQLL EDKIQRSVAF FMNIHARFLF EQRFHEARKN GALTVEVLNE
LMETAQKEAF VDSLKDYNPT FWQSKLHFYI DDIPFYNYPY TFGFLFSAGI YAQAASSETS
YEQAYIALLQ DTGSMTTENL AQKHLGVDLT QPDFWQAAVD VVLKDVTDFL ALTEDLI
//
