ID   TAGH_STAA8              Reviewed;         264 AA.
AC   Q2G2L1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Teichoic acids export ATP-binding protein TagH {ECO:0000255|HAMAP-Rule:MF_01715};
DE            EC=7.5.2.4 {ECO:0000255|HAMAP-Rule:MF_01715};
GN   Name=tagH {ECO:0000255|HAMAP-Rule:MF_01715};
GN   OrderedLocusNames=SAOUHSC_00641;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- FUNCTION: Part of the ABC transporter complex TagGH involved in
CC       teichoic acids export. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + teichoic acidSide 1 = ADP + phosphate + teichoic
CC         acidSide 2.; EC=7.5.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01715};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TagH) and
CC       two transmembrane proteins (TagG). {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01715};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Teichoic acids
CC       exporter (TC 3.A.1.104.1) family. {ECO:0000255|HAMAP-Rule:MF_01715}.
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DR   EMBL; CP000253; ABD29776.1; -; Genomic_DNA.
DR   RefSeq; WP_001103232.1; NZ_LS483365.1.
DR   RefSeq; YP_499201.1; NC_007795.1.
DR   AlphaFoldDB; Q2G2L1; -.
DR   SMR; Q2G2L1; -.
DR   STRING; 1280.SAXN108_0703; -.
DR   EnsemblBacteria; ABD29776; ABD29776; SAOUHSC_00641.
DR   GeneID; 3920049; -.
DR   KEGG; sao:SAOUHSC_00641; -.
DR   PATRIC; fig|93061.5.peg.575; -.
DR   eggNOG; COG1134; Bacteria.
DR   HOGENOM; CLU_000604_1_2_9; -.
DR   OMA; AVDAEFM; -.
DR   PRO; PR:Q2G2L1; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015438; F:ABC-type teichoic acid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03220; ABC_KpsT_Wzt; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015860; ABC_transpr_TagH-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51251; TAGH; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..264
FT                   /note="Teichoic acids export ATP-binding protein TagH"
FT                   /id="PRO_0000275851"
FT   DOMAIN          5..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT   BINDING         57..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
SQ   SEQUENCE   264 AA;  29763 MW;  F409CDD7BF79FAC4 CRC64;
     MNVSVNIKNV TKEYRIYRTN KERMKDALIP KHKNKTFFAL DDISLKAYEG DVIGLVGING
     SGKSTLSNII GGSLSPTVGK VDRNGEVSVI AISAGLSGQL TGIENIEFKM LCMGFKRKEI
     KAMTPKIIEF SELGEFIYQP VKKYSSGMRA KLGFSINITV NPDILVIDEA LSVGDQTFAQ
     KCLDKIYEFK EQNKTIFFVS HNLGQVRQFC TKIAWIEGGK LKDYGELDDV LPKYEAFLND
     FKKKSKAEQK EFRNKLDESR FVIK