ID   TCAA_STAHJ              Reviewed;         454 AA.
AC   Q4L8L4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Membrane-associated protein TcaA;
GN   Name=tcaA; OrderedLocusNames=SH0702;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04011.1; -; Genomic_DNA.
DR   RefSeq; WP_011275027.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8L4; -.
DR   SMR; Q4L8L4; -.
DR   STRING; 279808.SH0702; -.
DR   EnsemblBacteria; BAE04011; BAE04011; SH0702.
DR   KEGG; sha:SH0702; -.
DR   eggNOG; COG4640; Bacteria.
DR   HOGENOM; CLU_047245_0_0_9; -.
DR   OMA; KEYCKAD; -.
DR   OrthoDB; 370861at2; -.
DR   Proteomes; UP000000543; 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   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..454
FT                   /note="Membrane-associated protein TcaA"
FT                   /id="PRO_0000333175"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..454
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         4..21
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  50914 MW;  943860B923D7A852 CRC64;
     MSICPKCGQK IDSNLNKCPN CGNKLDNKDN QINSPQINTS NIRIRKFIPW AIVAFIIVLL
     IIVFVLVRNY NSPDAQTKIL VNAIDNNDSQ KVATLLSSKN SHIDSDEASV YIDYIRSEVG
     MKKFARDIKS TVETLNKSDS KEAINLKTRA GNNYLRVSKN GTRLLIFDNM SYTAPTKKAI
     VKPKLDTKYE FKDGGKKKTV IADANKTTSL GTYIPGIYSV DAKKETEYGE FSGQLKFDFR
     YGKSNTVEVN ENFNEALLTV KLKGKSDLDK DSLKVEINDK QMKYSSSREY GPYPQTKDVT
     VSALGKAKGK TFHAETKTIK ARDLGNINSA TLEFDDEEIS DYIEEKEAEE NSLKTKLSNF
     FSNYSFTLNS AISRSDFNLV STFLKDKSSI YKSIKNNLNQ SVAFINPQVI SASQKGNTIN
     TKVQHLNSNG QYETTNYELR EDSDTGNIQL VDSK