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Database: UniProt
Entry: Q65F60_BACLD
LinkDB: Q65F60_BACLD
Original site: Q65F60_BACLD 
ID   Q65F60_BACLD            Unreviewed;       594 AA.
AC   Q65F60; Q62QM5;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Peptidase M, neutral zinc metallopeptidases {ECO:0000313|EMBL:AAU24935.1};
GN   Name=yusX {ECO:0000313|EMBL:AAU24935.1};
GN   OrderedLocusNames=BL02187 {ECO:0000313|EMBL:AAU24935.1};
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU24935.1, ECO:0000313|Proteomes:UP000000606};
RN   [1] {ECO:0000313|EMBL:AAU24935.1, ECO:0000313|Proteomes:UP000000606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC   {ECO:0000313|Proteomes:UP000000606};
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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}.
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DR   EMBL; CP000002; AAU24935.1; -; Genomic_DNA.
DR   RefSeq; WP_003185092.1; NC_006322.1.
DR   AlphaFoldDB; Q65F60; -.
DR   STRING; 279010.BL02187; -.
DR   MEROPS; M03.A08; -.
DR   KEGG; bli:BL02187; -.
DR   PATRIC; fig|279010.13.peg.3529; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_3_1_9; -.
DR   Proteomes; UP000000606; Chromosome.
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:UP000000606};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          120..177
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          201..580
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   594 AA;  67026 MW;  F12E611FD1BDA174 CRC64;
     MTFHQLKDTW DLEVFFKGGS GSAEFRQYLN EIKTLLSTFK RSAEALTVSK SGLDELKETL
     ALFETIDVKI READAFVGCL QAQDTADLKA NALNFEVTRL AADAQKALVV LDSKFAVVPN
     VEWEAILQDE SISDIAYILN ERRERVTEKL SSEQETLIQG LSVDGYHAWG DMYDSIVDQI
     QIPYEEDGET KILSVGQAQN LTSKPDRKIR RSVSENLDHG WEQHADLLSS TLNHLAGFRL
     NVYEARGWDN VLKEPLDINR MKQETLDVMW QVIIDHKKPF ADYLSRKASL LGLDKLSWYD
     VEAPIGSAAK EYSYQEAAAF ITGQFKTFGK KLSSFAEKAL RDRWVEAEDR GGKRPGGFCA
     NFPDSGESRI FMTFAGSQSN VSTLAHELGH AFHQESMLDV RPLNRAYAMN VAETASTFAE
     MIVADAALKQ AGSDEEKIVL LEDKVQRSVA FFMNIHARFL FETRFYDERK NGVVSAGRLN
     ELMEEAQKEA FCGALGEYHP YFWASKLHFY ITSVPFYNFP YTFGYLFSLG IYAQALKEGA
     AFEEKYIALL KDTASMSVEE LAMKHLGADL TKRDFWEAAI QPAVRDAEAF LAMT
//
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