ID   TCAA_STAAT              Reviewed;         460 AA.
AC   A8Z547;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=USA300HOU_2338;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / TCH1516;
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA   Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA   Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA   Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA   Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
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   -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR   EMBL; CP000730; ABX30330.1; -; Genomic_DNA.
DR   RefSeq; WP_000833797.1; NC_010079.1.
DR   AlphaFoldDB; A8Z547; -.
DR   KEGG; sax:USA300HOU_2338; -.
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_0000333171"
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