LTAA_STAAW
ID LTAA_STAAW Reviewed; 396 AA.
AC Q8NXC4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Proton-coupled antiporter flippase LtaA {ECO:0000250|UniProtKB:Q2FZP8};
DE AltName: Full=Lipoteichoic acid protein A {ECO:0000250|UniProtKB:Q2FZP8};
GN Name=ltaA; OrderedLocusNames=MW0897;
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: Proton-coupled antiporter flippase that catalyzes the
CC translocation, from the inner to the outer leaflet of the cell
CC membrane, of the lipid-linked disaccharide (anchor-LLD) that anchors
CC lipoteichoic acids (LTA) to the cell membrane.
CC {ECO:0000250|UniProtKB:Q2FZP8}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q2FZP8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FZP8};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q2FZP8}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. LtaA family.
CC {ECO:0000305}.
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DR EMBL; BA000033; BAB94762.1; -; Genomic_DNA.
DR RefSeq; WP_001154224.1; NC_003923.1.
DR AlphaFoldDB; Q8NXC4; -.
DR SMR; Q8NXC4; -.
DR EnsemblBacteria; BAB94762; BAB94762; BAB94762.
DR KEGG; sam:MW0897; -.
DR HOGENOM; CLU_054518_0_0_9; -.
DR OMA; GYVYFAW; -.
DR UniPathway; UPA00556; -.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Antiport; Cell membrane; Lipid transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..396
FT /note="Proton-coupled antiporter flippase LtaA"
FT /id="PRO_0000287157"
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 44576 MW; 06AED17409A062C7 CRC64;
MQDSSLNNYA NHKNFILMLI ILFLMEFARG MYILSYINFL PTVTSIAVAI TSLAFSIHFI
ADASTNFVIG FLLKKFGTKI VLTTGFILAF TSLFLVIWFP ASPFVIIFSA MMLGIAVSPI
WVIMLSSVEE DKRGKQMGYV YFSWLLGLLV GMVFMNLLIK VHPTRFAFMM SLVVLIAWIL
YYFVDVKLTN YNTRPVKAQL RQIVDVTKRH LLLFPGILLQ GAAIAALVPI LPTYATKVIN
VSTIEYTVAI IIGGIGCAVS MLFLSKLIDN RSRNFMYGVI LSGFILYMIL IFTLSMIVNI
HIVWIIALAI GLMYGILLPA WNTFMARFIK SDEQEETWGV FNSIQGFGSM IGPLFGGLIT
QFTNNLNNTF YFSALIFLVL AVFYGSYFIA NREKAK