TCAA_STAEQ
ID TCAA_STAEQ Reviewed; 462 AA.
AC Q5HLN7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Membrane-associated protein TcaA;
GN Name=tcaA; OrderedLocusNames=SERP1948;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
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).
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; CP000029; AAW52830.1; -; Genomic_DNA.
DR RefSeq; WP_002470820.1; NC_002976.3.
DR AlphaFoldDB; Q5HLN7; -.
DR STRING; 176279.SERP1948; -.
DR EnsemblBacteria; AAW52830; AAW52830; SERP1948.
DR KEGG; ser:SERP1948; -.
DR eggNOG; COG4640; Bacteria.
DR HOGENOM; CLU_047245_0_0_9; -.
DR OMA; KEYCKAD; -.
DR OrthoDB; 370861at2; -.
DR Proteomes; UP000000531; 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 InterPro; IPR026870; Zinc_ribbon_dom.
DR Pfam; PF13240; zinc_ribbon_2; 1.
DR PIRSF; PIRSF032522; TcaA; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell membrane; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..462
FT /note="Membrane-associated protein TcaA"
FT /id="PRO_0000333174"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..462
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ZN_FING 4..21
FT /note="C4-type"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 52417 MW; B2F444551FBDC36D CRC64;
MSQCPNCGHQ VKDDTSQCPN CGQLLTKKKK RKIKDQSSQS SNENSTNIRL RKIVPIGISV
FILILIIVLF FLLRNYNSPN AQAKILVNAV DNNDSQKVAT LLSTKNKKVD DVEAQQYINY
VKKEVGIKKY IRDINNTVDK LNKSNSSVAS YIQTKSGQDV LKISKNGTKY LIFDNMSFTA
PTKKPIIKPK VETKYEFRTS GKKKTVIAEA NKNTPLGEFI PGTYHLPAKK ITENGTFNGH
LNFDFRESHS ETVDVAEDYD QSFINIKFKG ANKLSDKSEK VQINDRTFTY SHSKEFGPYP
KTKDITISAT GKAKGKTFSS ETKTISADDL KDNTKVTLEF DSDKINSYVE KKEKEENSLK
NKLTEFFTGY ATAMNSAFNM NDFNFISSYF KKNSSIYTSM KSNFQNRTNV TMISPQVLSV
HRNGHTVRTT IQHIDHIGNY INKDYELEID NDDSNMQLVK EL