TAGH_BACSU
ID TAGH_BACSU Reviewed; 527 AA.
AC P42954;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
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};
DE AltName: Full=Teichoic acid-transporting ATPase;
GN Name=tagH {ECO:0000255|HAMAP-Rule:MF_01715}; OrderedLocusNames=BSU35700;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168;
RX PubMed=7565096; DOI=10.1111/j.1365-2958.1995.tb02306.x;
RA Lazarevic V., Karamata D.;
RT "The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC
RT transporter involved in the metabolism of two wall teichoic acids.";
RL Mol. Microbiol. 16:345-355(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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, ECO:0000269|PubMed:7565096}.
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 -!- INTERACTION:
CC P42954; Q01467: mreD; NbExp=3; IntAct=EBI-6401700, EBI-5246853;
CC P42954; P42953: tagG; NbExp=3; IntAct=EBI-6401700, EBI-6401745;
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; U13832; AAB03363.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15587.1; -; Genomic_DNA.
DR PIR; S69203; S69203.
DR RefSeq; NP_391451.1; NC_000964.3.
DR RefSeq; WP_003227930.1; NZ_JNCM01000034.1.
DR PDB; 7DD0; X-ray; 2.70 A; A/B/C/D=1-280.
DR PDBsum; 7DD0; -.
DR AlphaFoldDB; P42954; -.
DR SMR; P42954; -.
DR IntAct; P42954; 7.
DR STRING; 224308.BSU35700; -.
DR TCDB; 3.A.1.104.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P42954; -.
DR PaxDb; P42954; -.
DR PRIDE; P42954; -.
DR EnsemblBacteria; CAB15587; CAB15587; BSU_35700.
DR GeneID; 936513; -.
DR KEGG; bsu:BSU35700; -.
DR PATRIC; fig|224308.179.peg.3865; -.
DR eggNOG; COG1134; Bacteria.
DR InParanoid; P42954; -.
DR OMA; CVDRINE; -.
DR BioCyc; BSUB:BSU35700-MON; -.
DR BioCyc; MetaCyc:BSU35700-MON; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..527
FT /note="Teichoic acids export ATP-binding protein TagH"
FT /id="PRO_0000092988"
FT DOMAIN 5..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT REGION 243..527
FT /note="Unknown"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:7DD0"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:7DD0"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:7DD0"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:7DD0"
SQ SEQUENCE 527 AA; 59244 MW; 48F7DD0911FB0EC3 CRC64;
MKLKVSFRNV SKQYHLYKKQ SDKIKGLFFP AKDNGFFAVR NVSFDVYEGE TIGFVGINGS
GKSTMSNLLA KIIPPTSGEI EMNGQPSLIA IAAGLNNQLT GRDNVRLKCL MMGLTNKEID
DMYDSIVEFA EIGDFINQPV KNYSSGMKSR LGFAISVHID PDILIIDEAL SVGDQTFYQK
CVDRINEFKK QGKTIFFVSH SIGQIEKMCD RVAWMHYGEL RMFDETKTVV KEYKAFIDWF
NKLSKKEKET YKKEQTEERK KEDPEAFARF RKKKKKPKSL ANAIQIAILS ILTVFMAGTM
FFNAPLRTIA SFGAIPQNEV KNHHGDAKGK SEERLTAINK QGFIANEKAA AYKDQGLKQK
ADVTLPFGTK VTVAAKGKQA AKIKFDGHSY YVKQSAVATN MKHAELHATA FTSYVSQNAA
SSYEYFLKFL GDSSTSIQSK LNGYTEGNKA DGRKTLNFDY EKISYVLEND KATELIFHNI
SPINPASLSL SDSDVLYDSS KKRFLVNTDD QVFAVDNEEH TLTLMLK
