TCAA_STAAM
ID TCAA_STAAM Reviewed; 460 AA.
AC Q99RS0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Membrane-associated protein TcaA;
GN Name=tcaA; OrderedLocusNames=SAV2356;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP INDUCTION BY VANCOMYCIN.
RX PubMed=16213099; DOI=10.1016/j.bbagen.2005.09.002;
RA Wootton M., Macgowan A.P., Walsh T.R.;
RT "Expression of tcaA and mprF and glycopeptide resistance in clinical
RT glycopeptide-intermediate Staphylococcus aureus (GISA) and heteroGISA
RT strains.";
RL Biochim. Biophys. Acta 1726:326-327(2005).
RN [3]
RP INDUCTION BY VANCOMYCIN.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: Weakly induced by vancomycin. {ECO:0000269|PubMed:16213099,
CC ECO:0000269|PubMed:16891058}.
CC -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR EMBL; BA000017; BAB58518.1; -; Genomic_DNA.
DR RefSeq; WP_000833794.1; NC_002758.2.
DR AlphaFoldDB; Q99RS0; -.
DR PaxDb; Q99RS0; -.
DR EnsemblBacteria; BAB58518; BAB58518; SAV2356.
DR KEGG; sav:SAV2356; -.
DR HOGENOM; CLU_047245_0_0_9; -.
DR OMA; RTYNWTY; -.
DR PhylomeDB; Q99RS0; -.
DR BioCyc; SAUR158878:SAV_RS12835-MON; -.
DR Proteomes; UP000002481; 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 Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..460
FT /note="Membrane-associated protein TcaA"
FT /id="PRO_0000333166"
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; 52131 MW; 089393362BCD78B4 CRC64;
MKSCPKCGQQ AQDDVQICTQ CGHKFDSRQA LYRKSTDEDI QTNNIKMRKM VPWAIGFFIL
ILIIILFFLL RNFNSPEAQT KILVNAIENN DKQKVATLLS TKDNKVDSEE AKVYINYIKD
EVGLKQFVSD LKNTVHKLNK SKTSVASYIQ TRSGQNILRV SKNGTRYIFF DNMSFTAPTK
QPIVKPKEKT KYEFKSGGKK KMVIAEANKV TPIGNFILGT YRIPAMKSTE NGDFAGYLKF
DFRQSNSETV DVTEDFEEAN ITVTLKGDTK LNDSSKKVTI NDREMAFSSS KTYGPYPQNK
DITISASGKA KGKTFTTQTK TIKASDLKYN TEITLNFDSE DIEDYVEKKE KEENSLKNKL
IEFFAGYSLA NNAAFNQSDF DFVSSYIKKG SSFYDDVKKR VSKGSLMMIS SPQIIDAEKH
GDKITATVRL INENGKQVDK EYELEQGSQD RLQLIKTSEK