TCAA_STAAW
ID TCAA_STAAW Reviewed; 460 AA.
AC Q8NV48;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Membrane-associated protein TcaA;
GN Name=tcaA; OrderedLocusNames=MW2277;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000033; BAB96142.1; -; Genomic_DNA.
DR RefSeq; WP_000833821.1; NC_003923.1.
DR AlphaFoldDB; Q8NV48; -.
DR SMR; Q8NV48; -.
DR EnsemblBacteria; BAB96142; BAB96142; BAB96142.
DR KEGG; sam:MW2277; -.
DR HOGENOM; CLU_047245_0_0_9; -.
DR OMA; RTYNWTY; -.
DR Proteomes; UP000000418; 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..460
FT /note="Membrane-associated protein TcaA"
FT /id="PRO_0000333167"
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; 52133 MW; F6026ED5E1F70045 CRC64;
MKSCSKCGQQ AQDDVQICTQ CGHKFDSRQA LYRKSTDEDI QTNNIKMRKM VPWAIGFFIL
ILIIILFFLL RNFNSPEAQT KILVNAIENN DKQKVATLLS TKDNKVDSEE AKVYINYIKD
EVGLKQFVSD LKNTVHKLNK SKTSVASYIQ TRSGQNILRV SKNGTRYIFF DNMSFTAPTK
QPIVKPKEKT KYEFKSGGKK KTVIAEANKV TPIGNFIPGT YRIPAMKSTE NGDFAGYLKF
DFRQSNSETV DVTEDFEEAN ITVTLKGDTK LNDSSKKVTI NDREMAFSSS KTYGPYPQNK
DITISASGKA KDKTFTTQTK TIKASDLKYN TEITLNFDSE DIEDYVEKKE KEENSLKNKL
IEFFAGYSLA NNAAFNQSDF DFVSSYIKKG SSFYDDVKKR VSKGSLMMIS SPQIIDAEKH
GDKITATVRL INENGKQVDK EYELEQGSQD RLQLIKTSEK