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TCAA_STAAE
ID   TCAA_STAAE              Reviewed;         460 AA.
AC   A6QJJ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=NWMN_2257;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   INDUCTION.
RX   PubMed=16891058; DOI=10.1016/j.bbagen.2006.06.008;
RA   McCallum N., Spehar G., Bischoff M., Berger-Bachi B.;
RT   "Strain dependence of the cell wall-damage induced stimulon in
RT   Staphylococcus aureus.";
RL   Biochim. Biophys. Acta 1760:1475-1481(2006).
CC   -!- FUNCTION: Plays a major role in decreasing resistance to glycopeptide
CC       antibiotics. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Induced by teicoplanin, vancomycin and oxacillin.
CC       {ECO:0000269|PubMed:16891058}.
CC   -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR   EMBL; AP009351; BAF68529.1; -; Genomic_DNA.
DR   RefSeq; WP_000833797.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QJJ7; -.
DR   EnsemblBacteria; BAF68529; BAF68529; NWMN_2257.
DR   KEGG; sae:NWMN_2257; -.
DR   HOGENOM; CLU_047245_0_0_9; -.
DR   OMA; RTYNWTY; -.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR023599; Mem_prot_TcaA.
DR   PIRSF; PIRSF032522; TcaA; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell membrane; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..460
FT                   /note="Membrane-associated protein TcaA"
FT                   /id="PRO_0000333170"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..460
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         4..21
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  52114 MW;  99B31F11D2987FC6 CRC64;
     MKSCPKCGQQ AQDDVQICTQ CGHKFDSRQA LYRKSTDEDI QTNNIKMRKM VPWAIGFFIL
     ILIIILFFLL RNFNSPEAQT KILVNAIENN DKQKVATLLS TKDNKVDSEE AKVYINYIKD
     EVGLKQFVSD LKNTVHKLNK SKTSVASYIQ TRSGQNILRV SKNGTRYIFF DNMSFTAPTK
     QPIVKPKEKT KYEFKSGGKK KMVIAEANKV TPIGNFIPGT YRIPAMKSTE NGDFAGHLKF
     DFRQSNSETV DVTEDFEEAN ISVTLKGDTK LNDSSKKVTI NDHEMAFSSS KTYGPYPQNK
     DITISASGKA KDKTFTTQTK TIKASDLKYN TEITLNFDSE DIEDYVEKKE KEENSLKNKL
     IEFFAGYSLA NNAAFNQSDF DFVSSYIKKG SSFYDDVKKR VSKGSLMMIS SPQIIDAEKH
     GDKITATVRL INENGKQVDK EYELEQGSQD RLQLIKTSEK
 
 
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