ID   TCAA_STAA8              Reviewed;         460 AA.
AC   Q2G2I1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=SAOUHSC_02635;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11042376; DOI=10.1016/s0304-4165(00)00133-1;
RA   Brandenberger M., Tschierske M., Giachino P., Wada A., Berger-Baechi B.;
RT   "Inactivation of a novel three-cistronic operon tcaR-tcaA-tcaB increases
RT   teicoplanin resistance in Staphylococcus aureus.";
RL   Biochim. Biophys. Acta 1523:135-139(2000).
RN   [3]
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).
RN   [4]
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:0000269|PubMed:11042376,
CC       ECO:0000269|PubMed:15155184}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Strongly induced by teicoplanin, vancomycin and oxacillin in
CC       strain RN4220, a restriction defective laboratory strain derived from
CC       NCTC 8325. {ECO:0000269|PubMed:16891058}.
CC   -!- DISRUPTION PHENOTYPE: Increased in resistance against glycopeptide
CC       antibiotics, especially teicoplanin. The resistance phenotype is
CC       lowered by several folds in strains carrying mutations in the rsbU gene
CC       which codes for a positive regulator of sigma-B.
CC       {ECO:0000269|PubMed:11042376, ECO:0000269|PubMed:15155184}.
CC   -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31644.1; -; Genomic_DNA.
DR   RefSeq; WP_000833797.1; NZ_LS483365.1.
DR   RefSeq; YP_501096.1; NC_007795.1.
DR   AlphaFoldDB; Q2G2I1; -.
DR   STRING; 1280.SAXN108_2607; -.
DR   EnsemblBacteria; ABD31644; ABD31644; SAOUHSC_02635.
DR   GeneID; 3921412; -.
DR   KEGG; sao:SAOUHSC_02635; -.
DR   PATRIC; fig|93061.5.peg.2383; -.
DR   eggNOG; COG4640; Bacteria.
DR   HOGENOM; CLU_047245_0_0_9; -.
DR   OMA; RTYNWTY; -.
DR   PRO; PR:Q2G2I1; -.
DR   Proteomes; UP000008816; 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   Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..460
FT                   /note="Membrane-associated protein TcaA"
FT                   /id="PRO_0000333169"
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