OPUCC_BACSU
ID OPUCC_BACSU Reviewed; 303 AA.
AC O32243; O31407;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glycine betaine/carnitine/choline-binding protein OpuCC;
DE AltName: Full=Osmoprotectant-binding protein;
DE Flags: Precursor;
GN Name=opuCC; Synonyms=yvbC; OrderedLocusNames=BSU33810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=168 / JH642;
RX PubMed=10216873; DOI=10.1046/j.1365-2958.1999.01354.x;
RA Kappes R.M., Kempf B., Kneip S., Boch J., Gade J., Meier-Wagner J.,
RA Bremer E.;
RT "Two evolutionarily closely related ABC transporters mediate the uptake of
RT choline for synthesis of the osmoprotectant glycine betaine in Bacillus
RT subtilis.";
RL Mol. Microbiol. 32:203-216(1999).
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).
RN [3]
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).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=23960087; DOI=10.1099/mic.0.067074-0;
RA Lee C.H., Wu T.Y., Shaw G.C.;
RT "Involvement of OpcR, a GbsR-type transcriptional regulator, in negative
RT regulation of two evolutionarily closely related choline uptake genes in
RT Bacillus subtilis.";
RL Microbiology 159:2087-2096(2013).
CC -!- FUNCTION: Member of a high affinity multicomponent binding-protein-
CC dependent transport system for glycine betaine, carnitine, and choline.
CC {ECO:0000269|PubMed:10216873, ECO:0000269|PubMed:8752321}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuCA),
CC two transmembrane proteins (OpuCB and OpuCD) and a solute-binding
CC protein (OpuCC). {ECO:0000269|PubMed:10216873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:10216873}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:10216873}.
CC -!- INDUCTION: Repressed by OpcR. {ECO:0000269|PubMed:23960087}.
CC -!- SIMILARITY: Belongs to the OsmX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF009352; AAB63770.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15386.1; -; Genomic_DNA.
DR PIR; E69670; E69670.
DR RefSeq; NP_391261.1; NC_000964.3.
DR RefSeq; WP_003228350.1; NZ_JNCM01000033.1.
DR PDB; 3PPN; X-ray; 2.30 A; A/B=1-303.
DR PDB; 3PPO; X-ray; 2.70 A; A/B=1-303.
DR PDB; 3PPP; X-ray; 2.40 A; A/B=1-303.
DR PDB; 3PPQ; X-ray; 1.91 A; A/B=1-303.
DR PDB; 3PPR; X-ray; 2.10 A; A/B=1-303.
DR PDBsum; 3PPN; -.
DR PDBsum; 3PPO; -.
DR PDBsum; 3PPP; -.
DR PDBsum; 3PPQ; -.
DR PDBsum; 3PPR; -.
DR AlphaFoldDB; O32243; -.
DR SMR; O32243; -.
DR STRING; 224308.BSU33810; -.
DR TCDB; 3.A.1.12.4; the atp-binding cassette (abc) superfamily.
DR PaxDb; O32243; -.
DR PRIDE; O32243; -.
DR EnsemblBacteria; CAB15386; CAB15386; BSU_33810.
DR GeneID; 936248; -.
DR KEGG; bsu:BSU33810; -.
DR PATRIC; fig|224308.43.peg.3544; -.
DR eggNOG; COG1732; Bacteria.
DR InParanoid; O32243; -.
DR OMA; KDPAWKN; -.
DR PhylomeDB; O32243; -.
DR BioCyc; BSUB:BSU33810-MON; -.
DR BRENDA; 7.6.2.9; 658.
DR EvolutionaryTrace; O32243; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0031460; P:glycine betaine transport; IBA:GO_Central.
DR InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR Pfam; PF04069; OpuAC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..303
FT /note="Glycine betaine/carnitine/choline-binding protein
FT OpuCC"
FT /id="PRO_0000031846"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="QL -> HV (in Ref. 1; AAB63770)"
FT /evidence="ECO:0000305"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:3PPQ"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3PPR"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3PPQ"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:3PPQ"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:3PPQ"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3PPQ"
SQ SEQUENCE 303 AA; 33957 MW; BEA28D72D7C7E2F9 CRC64;
MTKIKWLGAF ALVFVMLLGG CSLPGLGGAS DDTIKIGAQS MTESEIVANM IAQLIEHDTD
LNTALVKNLG SNYVQHQAML GGDIDISATR YSGTDLTSTL GKEAEKDPKK ALNIVQNEFQ
KRFSYKWFDS YGFDNTYAFT VTKKFAEKEH INTVSDLKKN ASQYKLGVDN AWLKRKGDGY
KGFVSTYGFE FGTTYPMQIG LVYDAVKNGK MDAVLAYSTD GRIKAYDLKI LKDDKRFFPP
YDCSPVIPEK VLKEHPELEG VINKLIGQID TETMQELNYE VDGKLKEPSV VAKEFLEKHH
YFD
