TAGH_STAHJ
ID TAGH_STAHJ Reviewed; 264 AA.
AC Q4L459;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
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}; OrderedLocusNames=SH2259;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05568.1; -; Genomic_DNA.
DR RefSeq; WP_011276519.1; NC_007168.1.
DR AlphaFoldDB; Q4L459; -.
DR SMR; Q4L459; -.
DR STRING; 279808.SH2259; -.
DR EnsemblBacteria; BAE05568; BAE05568; SH2259.
DR KEGG; sha:SH2259; -.
DR eggNOG; COG1134; Bacteria.
DR HOGENOM; CLU_000604_1_2_9; -.
DR OMA; VHIVYRV; -.
DR OrthoDB; 887953at2; -.
DR Proteomes; UP000000543; 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; Translocase;
KW Transport.
FT CHAIN 1..264
FT /note="Teichoic acids export ATP-binding protein TagH"
FT /id="PRO_0000275853"
FT DOMAIN 24..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; 29799 MW; 12550F2E90D4D790 CRC64;
MSVSVNINNV TKEYRIYRNN KERIKDALIP KNKNNTFFAL DDVSITAHEG DVIGLVGING
SGKSTLSNMI GGSISPTSGN IERNGEVSVI AINAGLNGRL TGVENIEFKM LCMGFKRKEI
KQLMPQVIEF SELGEFIHQP VKNYSSGMRA KLGFSINVTI NPDILVIDEA LSVGDQTFTQ
KCLDKIYEFK EANKTIFFVS HNIRQVREFC TKIAWIEGGK LKEYGDLEEV LPKYEQFLKD
FKKKSKADQK AFRKGLDEKR FIVK