(data stored in ACNUC7421 zone)

SWISSPROT: A5D3I7_PELTS

ID   A5D3I7_PELTS            Unreviewed;       670 AA.
AC   A5D3I7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=Membrane carboxypeptidase {ECO:0000313|EMBL:BAF59194.1};
GN   Name=MrcB {ECO:0000313|EMBL:BAF59194.1};
GN   OrderedLocusNames=PTH_1013 {ECO:0000313|EMBL:BAF59194.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59194.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-
RT   associated evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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DR   EMBL; AP009389; BAF59194.1; -; Genomic_DNA.
DR   STRING; 370438.PTH_1013; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; BAF59194; BAF59194; PTH_1013.
DR   KEGG; pth:PTH_1013; -.
DR   eggNOG; ENOG4105BZ4; Bacteria.
DR   eggNOG; COG0744; LUCA.
DR   HOGENOM; HOG000041137; -.
DR   KO; K21464; -.
DR   OMA; YAGKSGT; -.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   4: Predicted;
DR   PRODOM; A5D3I7.
DR   SWISS-2DPAGE; A5D3I7.
KW   Carboxypeptidase {ECO:0000313|EMBL:BAF59194.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006556};
KW   Hydrolase {ECO:0000313|EMBL:BAF59194.1};
KW   Protease {ECO:0000313|EMBL:BAF59194.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS01077424}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    670       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002680825.
FT   DOMAIN       44    219       Transgly. {ECO:0000259|Pfam:PF00912}.
FT   DOMAIN      308    579       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
SQ   SEQUENCE   670 AA;  72349 MW;  1643742D25F6356D CRC64;
     MTGKKSLFLA ACLFLLATGA GCSAQPFLMD ADVPPVSRIL DANGELIAAV SRENRIPVKL
     ENVSVFLREA IVAVEDARFY RHHGVDPVGV ARALYKNITA GRVVEGGSTI TQQLAKNLLP
     PEPERTAVRK LEELVLAVRL ERKYTKDEIL EMYLNQIYFG QGAYGVEAAA RTYFNKPAGE
     LNLAESAMLA GIPRAPSINN PVSNYEAAKA RQAVVLARMA ELGLISSGQA RQAMEERLQL
     AKKSPVLKKA PYFVDEVIRH FEISYPNGPE ILYAGGLTVY STLDLKIQRA AEKCLYEGLK
     NEDPLLDGAL VALDPKTGQI KAMAGGKDYS RSQFNRALSR IQPGSAFKPF LYAAAVERGY
     TAGTVINCEP VSFPQPDGTS YAPSDFHGSC HCRPFTLKEA LFTSDNVVAV RLNQSVGPSV
     TAGYARKMGI ESDLRAVPSL ALGTSEVTPL EMARAYGTLA NGGIKPEPYY IQKVTDSSGR
     ILEERRPQLE KAIDEKTAYI VTDMLEEVLG PGGTASNIAG ILDRPAAGKT GTTEEFREAW
     FVGYTPDLAA AVYVGFDEKS KSPGRSGAQL AAPIWANFMK EALKDVPPAG FAVPPGVVKA
     RICADDGLLA GEYNTRSIEA VFVRGTEPSA VCPGAGQLGP ADQVPPYYRM PLPGPEGLIL
     RRRLYFFGDD
//

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