TAGG_BACSU
ID TAGG_BACSU Reviewed; 275 AA.
AC P42953;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Teichoic acid translocation permease protein TagG;
GN Name=tagG; OrderedLocusNames=BSU35710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 (TC 3.A.1.34.1)
CC involved in exporting the two types of intracellularly synthesized
CC teichoic acids. Probably responsible for the translocation of the
CC substrate across the membrane.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TagH) and
CC two transmembrane proteins (TagG). {ECO:0000305}.
CC -!- INTERACTION:
CC P42953; P42954: tagH; NbExp=3; IntAct=EBI-6401745, EBI-6401700;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC {ECO:0000305}.
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DR EMBL; U13832; AAB03362.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15588.1; -; Genomic_DNA.
DR PIR; S69202; S69202.
DR RefSeq; NP_391452.1; NC_000964.3.
DR RefSeq; WP_003227928.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42953; -.
DR SMR; P42953; -.
DR IntAct; P42953; 1.
DR STRING; 224308.BSU35710; -.
DR TCDB; 3.A.1.104.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P42953; -.
DR EnsemblBacteria; CAB15588; CAB15588; BSU_35710.
DR GeneID; 936794; -.
DR KEGG; bsu:BSU35710; -.
DR PATRIC; fig|224308.179.peg.3866; -.
DR eggNOG; COG1682; Bacteria.
DR InParanoid; P42953; -.
DR OMA; GFAWFQK; -.
DR PhylomeDB; P42953; -.
DR BioCyc; BSUB:BSU35710-MON; -.
DR BioCyc; MetaCyc:BSU35710-MON; -.
DR PRO; PR:P42953; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015920; P:lipopolysaccharide transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR000412; ABC_2_transport.
DR Pfam; PF01061; ABC2_membrane; 1.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..275
FT /note="Teichoic acid translocation permease protein TagG"
FT /id="PRO_0000182996"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..267
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ SEQUENCE 275 AA; 32185 MW; 8305729ACDCB88D5 CRC64;
MNDLLRILRE QITSFPLILR LAAYETKSKY QMNYLGVLWQ FLNPLIQMLA YWFVFGMGIR
KGGPVTTGAG EVPFIIWMLA GLIPWFFISP TILDGSNSVF KRINMVAKMN FPISSLPSVA
IASNLFSYMI MMVIYIIVLL VNGVFPSVHW LQYIYYFICM IAFMFSFSLF NSTISVLIRD
YQFLLQAVTR LLFFLLPIFW DVNAKLGQSH PELVPVLKLN PLFYIIEGFR NSFLDGAWFF
HDMKYTLYFW LFTFLLLLVG SILHMKFRDK FVDFL
