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Database: UniProt
Entry: Q7UFS8_RHOBA
LinkDB: Q7UFS8_RHOBA
Original site: Q7UFS8_RHOBA 
ID   Q7UFS8_RHOBA            Unreviewed;       401 AA.
AC   Q7UFS8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Peptidase, M20A family {ECO:0000313|EMBL:CAD78602.1};
DE            EC=3.4.11.- {ECO:0000313|EMBL:CAD78602.1};
GN   Name=pepT {ECO:0000313|EMBL:CAD78602.1};
GN   OrderedLocusNames=RB8363 {ECO:0000313|EMBL:CAD78602.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78602.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78602.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; BX294147; CAD78602.1; -; Genomic_DNA.
DR   RefSeq; NP_868324.1; NC_005027.1.
DR   RefSeq; WP_011121827.1; NC_005027.1.
DR   AlphaFoldDB; Q7UFS8; -.
DR   STRING; 243090.RB8363; -.
DR   EnsemblBacteria; CAD78602; CAD78602; RB8363.
DR   KEGG; rba:RB8363; -.
DR   PATRIC; fig|243090.15.peg.4026; -.
DR   eggNOG; COG2195; Bacteria.
DR   HOGENOM; CLU_021802_6_0_0; -.
DR   InParanoid; Q7UFS8; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR42994; PEPTIDASE T; 1.
DR   PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:CAD78602.1};
KW   Hydrolase {ECO:0000313|EMBL:CAD78602.1};
KW   Protease {ECO:0000313|EMBL:CAD78602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT   DOMAIN          200..296
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   401 AA;  42467 MW;  7094FC0D176BF3C0 CRC64;
     MSWAAIDESA ALDRFLELTR IPGKSGDEAA ISAAIEKMLV DAGVDPDWIQ SDDAGTKTRL
     DGNAGNLIVT LPGDDSLPRT LLSAHMDTVP ICVGCNPQLR DDDQLGRIVV ADGPTGLGAD
     DRSGCAVILS AIVERLSRQA KNPDLKLAPA AVTFLIQEEV GLEGARHLDV SKVGHVDRAF
     NFDGGALDKI RHGAIGGERV QVTIHGHAAH AGVAPEKGVS AIVIASEAIS SLHRNGWLGL
     VEKDGRRGTA NVGVFQGGDA TNVITPEVQL RAEARSHDAE FRAEIVSQMR TAIENAVQSV
     KDVQGRTGSF EFTSRVDYEA FRLAEDHPSV LAATELISQL GRSPQCEVAN GGLDANWLML
     HGIEAVTLGC GQASIHTVDE YLMVDEFLDA CRLAAELIAP A
//
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