TAGH_STAAR
ID TAGH_STAAR Reviewed; 264 AA.
AC Q6GJ33;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SAR0647;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39664.1; -; Genomic_DNA.
DR RefSeq; WP_001103233.1; NC_002952.2.
DR AlphaFoldDB; Q6GJ33; -.
DR SMR; Q6GJ33; -.
DR KEGG; sar:SAR0647; -.
DR HOGENOM; CLU_000604_1_2_9; -.
DR OMA; AVDAEFM; -.
DR OrthoDB; 887953at2; -.
DR Proteomes; UP000000596; 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_0000092998"
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; 29748 MW; 840F7B67B9C9FAC0 CRC64;
MNVSVNIKNV TKEYRIYRTN KERMKDALIP KHKNKTFFAL DDISLKAYEG DVIGLVGING
SGKSTLSNII GGSLSPTVGK VDRNGEVSVI AISAGLSGQL TGIENIEFKM LCMGFKRKEI
KAMTPKIIEF SELGEFIYQP VKKYSSGMRA KLGFSINITV NPDILVIDEA LSVGDQTFAQ
KCLDNIYEFK EQNKTIFFVS HNLGQVRQFC TKIAWIEGGK LKDYGELDDV LPKYEAFLND
FKKKSKAEQK EFRNKLDESR FVIK