TCAA_STAAC
ID TCAA_STAAC Reviewed; 460 AA.
AC Q5HDJ9; Q9F4G2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Membrane-associated protein TcaA;
DE AltName: Full=Teicoplanin-associated protein A;
GN Name=tcaA; OrderedLocusNames=SACOL2352;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11042376; DOI=10.1016/s0304-4165(00)00133-1;
RA Brandenberger M., Tschierske M., Giachino P., Wada A., Berger-Baechi B.;
RT "Inactivation of a novel three-cistronic operon tcaR-tcaA-tcaB increases
RT teicoplanin resistance in Staphylococcus aureus.";
RL Biochim. Biophys. Acta 1523:135-139(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [3]
RP FUNCTION IN TEICOPLANIN SUSCEPTIBILITY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15155184; DOI=10.1128/aac.48.6.1953-1959.2004;
RA Maki H., McCallum N., Bischoff M., Wada A., Berger-Baechi B.;
RT "TcaA inactivation increases glycopeptide resistance in Staphylococcus
RT aureus.";
RL Antimicrob. Agents Chemother. 48:1953-1959(2004).
RN [4]
RP INDUCTION.
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).
RN [5]
RP TOPOLOGY.
RX PubMed=17709474; DOI=10.1128/aac.00722-07;
RA McCallum N., Brassinga A.K.C., Sifri C.D., Berger-Baechi B.;
RT "Functional characterization of tcaA: minimal requirement for teicoplanin
RT susceptibility and role in Caenorhabditis elegans virulence.";
RL Antimicrob. Agents Chemother. 51:3836-3843(2007).
CC -!- FUNCTION: Plays a major role in decreasing resistance to glycopeptide
CC antibiotics. Overexpression confers oxacillin hypersusceptibility,
CC without affecting the levels of resistance towards vancomycin. Could be
CC involved in virulence. Overexpression increases the levels of
CC teicoplanin susceptibility. Overexpression also increased
CC susceptibility to oxacillin in methicillin-resistant strains.
CC {ECO:0000269|PubMed:15155184}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- INDUCTION: Strongly up-regulated by teicoplanin and vancomycin even at
CC lower concentrations (10 ug/ml). Induced by oxacillin at a very high
CC concentration of over 1000 ug/ml. {ECO:0000269|PubMed:15155184,
CC ECO:0000269|PubMed:16891058}.
CC -!- DISRUPTION PHENOTYPE: Increased resistance against glycopeptide
CC antibiotics, especially teicoplanin. {ECO:0000269|PubMed:15155184}.
CC -!- SIMILARITY: Belongs to the TcaA family. {ECO:0000305}.
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DR EMBL; AY008833; AAG23888.1; -; Genomic_DNA.
DR EMBL; CP000046; AAW37180.1; -; Genomic_DNA.
DR RefSeq; WP_000833786.1; NC_002951.2.
DR AlphaFoldDB; Q5HDJ9; -.
DR SMR; Q5HDJ9; -.
DR EnsemblBacteria; AAW37180; AAW37180; SACOL2352.
DR KEGG; sac:SACOL2352; -.
DR HOGENOM; CLU_047245_0_0_9; -.
DR OMA; RTYNWTY; -.
DR PHI-base; PHI:7918; -.
DR Proteomes; UP000000530; 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 1: Evidence at protein 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_0000333160"
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"
FT REGION 49..177
FT /note="Required for teicoplanin susceptibility"
SQ SEQUENCE 460 AA; 52148 MW; FDF3B9F283F7EC08 CRC64;
MKSCPKCGQQ AQDDVQICTQ CGHKFDSRQA FYRKSTDEDI 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
