TAGH_STAAM
ID TAGH_STAAM Reviewed; 264 AA.
AC Q7A2W2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SAV0637;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56799.1; -; Genomic_DNA.
DR RefSeq; WP_001103231.1; NC_002758.2.
DR AlphaFoldDB; Q7A2W2; -.
DR SMR; Q7A2W2; -.
DR World-2DPAGE; 0002:Q7A2W2; -.
DR PaxDb; Q7A2W2; -.
DR EnsemblBacteria; BAB56799; BAB56799; SAV0637.
DR KEGG; sav:SAV0637; -.
DR HOGENOM; CLU_000604_1_2_9; -.
DR OMA; AVDAEFM; -.
DR PhylomeDB; Q7A2W2; -.
DR BioCyc; SAUR158878:SAV_RS03515-MON; -.
DR Proteomes; UP000002481; 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_0000092996"
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