ID W4DB50_9BACL Unreviewed; 598 AA.
AC W4DB50;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase M3 family protein {ECO:0000313|EMBL:ETT64967.1};
GN ORFNames=C173_20769 {ECO:0000313|EMBL:ETT64967.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT64967.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT64967.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT64967.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(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:ETT64967.1}.
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DR EMBL; ASPX01000070; ETT64967.1; -; Genomic_DNA.
DR RefSeq; WP_036728011.1; NZ_ASPX01000070.1.
DR AlphaFoldDB; W4DB50; -.
DR PATRIC; fig|1227352.4.peg.4159; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000019051; 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; 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 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 Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 118..182
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..585
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 598 AA; 66738 MW; 2FC4AB4280F3CE98 CRC64;
MESTTCELTW NLDRIYPSFE SEGFQQDRRQ VESLAGELNT WSASQPVSGQ APAELMEEFL
KQYNAYQQLY LRLFSYAELR FSADSQCEEA VNLMDELEEV TSGAGEALVR FSKWLAGVSA
DELERSLRFS AYLEQHSFYL RGLQGKSQHM LSAEGEAVIA RMQNTGSKAW ERLYMQTLST
LRTDLELAGV TRSVTLAELR NLVYDPDPAV RRAAAEAEHE ACRSVAEQSA ACINAVSGEA
AAIYELRGYA SPLHKVLEAA RMDEETLEVM LQAIRESLPV FREYYAEKAG RLGHSGGQLP
FWDVFAPIGT ESSIRVTYAE AQAMIIAGFS RFSPELGGFA RKVFGERWID AEPRSGKGNF
GMCVDIVPIG ESRIITSFHG QYIDVSVLAH EIGHAYHTSR LAGYTMVNMD YPVPIAETAS
IFCESLIHVE LLNSLPAEEA DAILERSLSD AGYYIVDFYA RYCFESALYA RRLSGPLPLE
ELNALMLESM AAAYGDSVLP GSIHPYQWIS KAGYYMAGNE FLNFPYSFGL LFSKGLYAQY
QKQGQAFVSR YEQFLSATST RSIADAAKLM DIDVHSLDFW QEALGFIAGD VRKFAGRE
//
