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Database: UniProt
Entry: I8RPB4_9FIRM
LinkDB: I8RPB4_9FIRM
Original site: I8RPB4_9FIRM 
ID   I8RPB4_9FIRM            Unreviewed;       381 AA.
AC   I8RPB4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Peptidase dimerization domain protein {ECO:0000313|EMBL:EIW21010.1};
GN   ORFNames=FB4_1862 {ECO:0000313|EMBL:EIW21010.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW21010.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW21010.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW21010.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
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:EIW21010.1}.
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DR   EMBL; AKVJ01000002; EIW21010.1; -; Genomic_DNA.
DR   RefSeq; WP_007930376.1; NZ_AKVJ01000002.1.
DR   AlphaFoldDB; I8RPB4; -.
DR   PATRIC; fig|1149862.3.peg.138; -.
DR   OrthoDB; 9783294at2; -.
DR   Proteomes; UP000004324; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03885; M20_CPDG2; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          179..277
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   381 AA;  41162 MW;  0DE9813A722A4830 CRC64;
     MEIKKLEVSS YLEELEYLVN IDSVSSDAAG TAKIAEFMTA KYRSLGWQVK EHQFNNTIGP
     CLEITNKAAE QYEVLILAHM DTVFPIGTAK ERPFFIKDGR AYGPGVVDCK AGLLSGFYAL
     AALETMGKLE DRAVCVFLNS DHEGISSKYS KFHSEELAKQ SKCTLVIEAA RANGNLVHKR
     KGIGRYYIEV DGVAAHAGVD HQKGCNAIEE IAHWVLALQG RTDYAKETTL NIGKISGGTS
     ISAVPDKAKA ELDIRFYDEK AVTVIEQLMK DLAAQPHVAG TTANVVGGIT RPSMVPSEKT
     EELVHAIDEI GKSLQIDFGW TASGGGSDGS FSAAAGTPTI DGLGPVGGGA HSSQEYLEID
     TVVPRYELLC KIIAYVVNWK K
//
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