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TCAA_STAA1
ID   TCAA_STAA1              Reviewed;         460 AA.
AC   A7X5X6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=SAHV_2340;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15155184; DOI=10.1128/aac.48.6.1953-1959.2004;
RA   Maki H., McCallum N., Bischoff M., Wada A., Berger-Baechi B.;
RT   "TcaA inactivation increases glycopeptide resistance in Staphylococcus
RT   aureus.";
RL   Antimicrob. Agents Chemother. 48:1953-1959(2004).
CC   -!- FUNCTION: Plays a major role in decreasing resistance to glycopeptide
CC       antibiotics. {ECO:0000269|PubMed:15155184}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Increased resistance to teicoplanin and
CC       vancomycin. {ECO:0000269|PubMed:15155184}.
CC   -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR   EMBL; AP009324; BAF79223.1; -; Genomic_DNA.
DR   RefSeq; WP_000833794.1; NC_009782.1.
DR   AlphaFoldDB; A7X5X6; -.
DR   KEGG; saw:SAHV_2340; -.
DR   HOGENOM; CLU_047245_0_0_9; -.
DR   OMA; RTYNWTY; -.
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   3: Inferred from homology;
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_0000333165"
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;  52131 MW;  089393362BCD78B4 CRC64;
     MKSCPKCGQQ AQDDVQICTQ CGHKFDSRQA LYRKSTDEDI QTNNIKMRKM VPWAIGFFIL
     ILIIILFFLL RNFNSPEAQT KILVNAIENN DKQKVATLLS TKDNKVDSEE AKVYINYIKD
     EVGLKQFVSD LKNTVHKLNK SKTSVASYIQ TRSGQNILRV SKNGTRYIFF DNMSFTAPTK
     QPIVKPKEKT KYEFKSGGKK KMVIAEANKV TPIGNFILGT YRIPAMKSTE NGDFAGYLKF
     DFRQSNSETV DVTEDFEEAN ITVTLKGDTK LNDSSKKVTI NDREMAFSSS KTYGPYPQNK
     DITISASGKA KGKTFTTQTK TIKASDLKYN TEITLNFDSE DIEDYVEKKE KEENSLKNKL
     IEFFAGYSLA NNAAFNQSDF DFVSSYIKKG SSFYDDVKKR VSKGSLMMIS SPQIIDAEKH
     GDKITATVRL INENGKQVDK EYELEQGSQD RLQLIKTSEK
 
 
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