ID   TAGH_STAAU              Reviewed;         264 AA.
AC   Q9LC44;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
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};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NU3-1;
RX   PubMed=10754251; DOI=10.1111/j.1574-6968.2000.tb09065.x;
RA   Horii T., Yokoyama K., Barua S., Odagiri T., Futamura N., Hasegawa T.,
RA   Ohta M.;
RT   "The staphylokinase gene is located in the structural gene encoding N-
RT   acetylmuramyl-L-alanine amidase in methicillin-resistant Staphylococcus
RT   aureus.";
RL   FEMS Microbiol. Lett. 185:221-224(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB033232; BAA95013.1; -; Genomic_DNA.
DR   PIR; F89833; F89833.
DR   RefSeq; WP_001103231.1; NZ_WYDB01000004.1.
DR   AlphaFoldDB; Q9LC44; -.
DR   SMR; Q9LC44; -.
DR   PRIDE; Q9LC44; -.
DR   OMA; AVDAEFM; -.
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; Translocase;
KW   Transport.
FT   CHAIN           1..264
FT                   /note="Teichoic acids export ATP-binding protein TagH"
FT                   /id="PRO_0000093000"
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;  29747 MW;  F409CDD7BF619AC4 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 EFRNKLDEAR FVIK