ID W1SRR2_9BACI Unreviewed; 565 AA.
AC W1SRR2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=M3 family oligoendopeptidase {ECO:0000313|EMBL:ETI69798.1};
GN ORFNames=BAVI_05754 {ECO:0000313|EMBL:ETI69798.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI69798.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI69798.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI69798.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(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:ETI69798.1}.
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DR EMBL; ALAN01000039; ETI69798.1; -; Genomic_DNA.
DR RefSeq; WP_024027365.1; NZ_ALAN01000039.1.
DR AlphaFoldDB; W1SRR2; -.
DR STRING; 220686.AA980_12215; -.
DR PATRIC; fig|1131730.3.peg.1217; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000018877; 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; cd09606; M3B_PepF; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR NCBIfam; TIGR02289; M3_not_pepF; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 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:UP000018877};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 174..515
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 565 AA; 66000 MW; 6C5121CFE0E2E615 CRC64;
MTQDLNQNYY KELIDLQDVD GVEAQIQSLL DVQIESVSDL EKWLQAEKDL MMKIAEAMTG
HQVDFYRNTE DADIKSTYLH DQQVIQPLLM KYEAKLNQKV CESPYFNKLD ENRYGLMRRF
RESKVKLFRE ENIPLMVKEQ ELNTKYSEIM GGLTVEWDDE EKPYPFIQSQ LDHLDRAVRE
KAYRAMMSAH RQIKPDMDAI MDELVQLRHQ IALNAGFENY RDYMFVVKNR EYSVQDCYDF
HENVEKHIIP AWNRLANVFK SELGVDTFRP WDNTAKLMKN PPYSDVSDLM NGVSEMLGKT
DPYFADRFDY MREHGLIDLG DRKGKSPGGF CTSLPVSGDT FVFANFSPSF FSLIALIHEM
GHAVNGYLEF SEQGPSEEYH LRMEIGELYS HGMELLLLDK LDRFYPEEED FKSAQREELR
RAFKMLFGPL SGDLFQHWMY TNPQHTAKER DEKFFEISKR YGLNPVDTSG LEKEIGMSWA
DTLHYFQVPF YNIEYSMSML GALQILENYR NNPEQAVVSF KKGASANYNQ SIAAVYKETG
VSFDFSEPAV KRMGEFLEKV IQDIH
//
