OPUAB_BACSU
ID OPUAB_BACSU Reviewed; 282 AA.
AC P46921;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glycine betaine transport system permease protein OpuAB;
GN Name=opuAB; OrderedLocusNames=BSU02990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=168 / JH642;
RX PubMed=7622480; DOI=10.1074/jbc.270.28.16701;
RA Kempf B., Bremer E.;
RT "OpuA, an osmotically regulated binding protein-dependent transport system
RT for the osmoprotectant glycine betaine in Bacillus subtilis.";
RL J. Biol. Chem. 270:16701-16713(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [3]
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).
RN [4]
RP FUNCTION IN GLYCINE BETAINE TRANSPORT.
RC STRAIN=168 / JH642;
RX PubMed=8752321; DOI=10.1128/jb.178.17.5071-5079.1996;
RA Kappes R., Kempf B., Bremer E.;
RT "Three transport systems for the osmoprotectant glycine betaine operate in
RT Bacillus subtilis: characterization of OpuD.";
RL J. Bacteriol. 178:5071-5079(1996).
CC -!- FUNCTION: Involved in a multicomponent binding-protein-dependent
CC transport system for glycine betaine; probably responsible for the
CC translocation of the substrate across the membrane.
CC {ECO:0000269|PubMed:7622480, ECO:0000269|PubMed:8752321}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuAA),
CC two transmembrane proteins (OpuAB) and a solute-binding protein
CC (OpuAC). {ECO:0000269|PubMed:7622480}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; U17292; AAC43456.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08933.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12093.1; -; Genomic_DNA.
DR PIR; I40536; I40536.
DR RefSeq; NP_388181.1; NC_000964.3.
DR RefSeq; WP_003234703.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P46921; -.
DR SMR; P46921; -.
DR STRING; 224308.BSU02990; -.
DR TCDB; 3.A.1.12.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P46921; -.
DR EnsemblBacteria; CAB12093; CAB12093; BSU_02990.
DR GeneID; 938360; -.
DR KEGG; bsu:BSU02990; -.
DR PATRIC; fig|224308.179.peg.311; -.
DR eggNOG; COG4176; Bacteria.
DR InParanoid; P46921; -.
DR OMA; HFNIMDP; -.
DR PhylomeDB; P46921; -.
DR BioCyc; BSUB:BSU02990-MON; -.
DR BRENDA; 7.6.2.9; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR GO; GO:0015871; P:choline transport; IBA:GO_Central.
DR GO; GO:0031460; P:glycine betaine transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..282
FT /note="Glycine betaine transport system permease protein
FT OpuAB"
FT /id="PRO_0000060153"
FT TOPO_DOM 1..18
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 40..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 66..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 91..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 115..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 159..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 237..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 264..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 90..269
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 282 AA; 30247 MW; B05FDABD403BDBC1 CRC64;
MDRLPRIPLA DIIDRFVDWI TMTFGGFFDG IANGLAAFVN GIVTGLGFIP SILLTIIFAA
LAWWISTRGI ALFTLIGFLL IDYLGYWDPM LQTLALVLTS VIISIVVGVP IGIWASQKET
VRRIVTPILD LMQTMPAFVY LLPAIFFFNI GVVPGVVASV IFAMPPTIRM TVLGIKQVPA
DLIEATEAFG STTAQRLFKV QLPLATKTIL AGINQSIMLA LSMVVIAAMV GAPGLGSEVY
SAVTQLKTGV GVEAGIAIVI VAITLDRITQ NIKVKKKSRG NA
