ID   TCAA_STAA9              Reviewed;         460 AA.
AC   A5IVD7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=SaurJH9_2380;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH9;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH9.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INDUCTION.
RX   PubMed=16428416; DOI=10.1128/jb.188.3.1120-1133.2006;
RA   McAleese F., Wu S.W., Sieradzki K., Dunman P., Murphy E., Projan S.,
RA   Tomasz A.;
RT   "Overexpression of genes of the cell wall stimulon in clinical isolates of
RT   Staphylococcus aureus exhibiting vancomycin-intermediate-S. aureus-type
RT   resistance to vancomycin.";
RL   J. Bacteriol. 188:1120-1133(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 cell wall active antibiotics oxacillin, D-
CC       cycloserine or bacitracin. {ECO:0000269|PubMed:16428416}.
CC   -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR   EMBL; CP000703; ABQ50160.1; -; Genomic_DNA.
DR   RefSeq; WP_000833818.1; NC_009487.1.
DR   AlphaFoldDB; A5IVD7; -.
DR   SMR; A5IVD7; -.
DR   KEGG; saj:SaurJH9_2380; -.
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   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_0000333162"
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;  52157 MW;  4C778C39D84FFC3C CRC64;
     MKSCPKCGQQ AQDDVQICTQ CGHKFDSRQA LYRKSTDEDI QTNNIKMRKM VPWAIVFFIL
     ILIIILFFLL RNFNSPEAQT KILVNAIENN DKQKVATLLS TKDNKVDSEE AKVYINYIKD
     EVGLKQFVSD LKNTVHKLNK SKTSVASYIQ TRSGQNILRV SKNGTRYIFF DNMSFTAPTK
     QPIVKPKEKT KYEFKSGGKK KMVIAEANKV TPIGNFIPGT YRIPAMKSTE NGDFAGYLKF
     DFRQSNSETV DVTEDFEEAN ITVTLKGDTK LNDSSKKVTI NDREMAFSSS KTYGPYPQNK
     DITISASGKA KGKTFTTQTK TIKASDLKYN TEITLNFDSE DIEDYVEKKE KEENSLKNKL
     IEFFAGYSLA NNAAFNQSDF DFVSSYIKKG SSFYDDVKKR VSKGSLMMIS SPQIIDAEKH
     GDKITATVRL INENGKQVDK EYELEQGSQD RLQLIKTSEK