(data stored in SCRATCH zone)

SWISSPROT: A4F6Q9_SACEN

ID   A4F6Q9_SACEN            Unreviewed;       667 AA.
AC   A4F6Q9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   SubName: Full=Membrane carboxypeptidase, penicillin-binding protein {ECO:0000313|EMBL:CAL99733.1};
DE            EC=2.4.2.- {ECO:0000313|EMBL:CAL99733.1};
DE   SubName: Full=Membrane peptidoglycan carboxypeptidase {ECO:0000313|EMBL:PFG93536.1};
GN   Name=mrcB {ECO:0000313|EMBL:CAL99733.1};
GN   OrderedLocusNames=SACE_0385 {ECO:0000313|EMBL:CAL99733.1};
GN   ORFNames=A8924_0781 {ECO:0000313|EMBL:PFG93536.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99733.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99733.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99733.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93536.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93536.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AM420293; CAL99733.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93536.1; -; Genomic_DNA.
DR   RefSeq; WP_011873039.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0385; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; CAL99733; CAL99733; SACE_0385.
DR   KEGG; sen:SACE_0385; -.
DR   eggNOG; ENOG4105BZ4; Bacteria.
DR   eggNOG; COG0744; LUCA.
DR   HOGENOM; HOG000041137; -.
DR   OMA; TEITIMP; -.
DR   OrthoDB; 652304at2; -.
DR   BioCyc; SERY405948:SACE_RS01890-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 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; A4F6Q9.
DR   SWISS-2DPAGE; A4F6Q9.
KW   Carboxypeptidase {ECO:0000313|EMBL:CAL99733.1};
KW   Glycosyltransferase {ECO:0000313|EMBL:CAL99733.1};
KW   Hydrolase {ECO:0000313|EMBL:CAL99733.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CAL99733.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Transferase {ECO:0000256|SAAS:SAAS01077424, ECO:0000313|EMBL:CAL99733.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..246
FT                   /note="Transgly"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          342..594
FT                   /note="Transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          509..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..525
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  71638 MW;  27C147DABE839FF9 CRC64;
     MSDDATTVLV PAARRRRRLR RALRASVFTA TALLLGAVGA FAVGYAVWEV PDPRAVATGT
     QQSIVLQYAD GTEMTRIVPG TGNRTMIGSL HEVSPAMRQA TLAAEDASFY SNGGFDVLGI
     VRAAYAQLTD SPGGGSTLTQ QYIKLATGED EHTYTRKFKE IVLSAKMTNE QPKDEIFKAY
     LNTAYYGRGA WGVHAASNAY FGKLPRDLDA SEAAVLAGAV QKPTENDPRV NAAQAAKRWE
     YVADQMLANH MITGEQRRRM AVPPTRERFA WRGEEMSGPL FHIRERVLEE LERDGLTARD
     MHRDGNTVVT NIDRDAQRAA EEAVAAMTEG RSQNLRSALV SIEPGTGAIR AYHSGDREIG
     GFDWARAAQP PGAAMQPFVV AAGLMRGHGL AETYDGTSPH EIMGATYRNS GVDCSRTCTA
     RMAMAEASET AFVNMAAKFG PAAVLDAAQR AGMRVDTGDD GRRVGLGIAT GDYPVSTVDV
     ARGYATLAAG GADHEPRFVR RVLDRTGNEV RSFEPEPRTA FGDDPEMSRD VSGNVTESLS
     WSAWGTNWAL DGKRPVAVKS GIAQFGGSPD EAVTAWTAGY TPQIATAVSL SASDERGRPQ
     PVVDATSSQA GDVLTGPTWQ RFMNAYLADE PVEPFPDFGP VGRYAEPSGV PFPPVTTSVP
     LPPLADR
//

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