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Protein

Glycine betaine/carnitine/choline-binding protein OpuCC

Gene

opuCC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciBSUB:BSU33810-MONOMER.
BRENDAi3.6.3.32. 658.

Protein family/group databases

TCDBi3.A.1.12.4. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine betaine/carnitine/choline-binding protein OpuCC
Alternative name(s):
Osmoprotectant-binding protein
Gene namesi
Name:opuCC
Synonyms:yvbC
Ordered Locus Names:BSU33810
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane PROSITE-ProRule annotation1 Publication; Lipid-anchor PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020PROSITE-ProRule annotationAdd
BLAST
Chaini21 – 303283Glycine betaine/carnitine/choline-binding protein OpuCCPRO_0000031846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteineCurated
Lipidationi21 – 211S-diacylglycerol cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiO32243.

Expressioni

Inductioni

Repressed by OpcR.1 Publication

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (OpuCA), two transmembrane proteins (OpuCB and OpuCD) and a solute-binding protein (OpuCC).1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018341.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 418Combined sources
Helixi42 – 5817Combined sources
Beta strandi63 – 697Combined sources
Helixi72 – 809Combined sources
Beta strandi85 – 917Combined sources
Helixi92 – 976Combined sources
Turni98 – 1003Combined sources
Helixi108 – 12316Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi137 – 1426Combined sources
Helixi143 – 1497Combined sources
Beta strandi152 – 1543Combined sources
Helixi155 – 1639Combined sources
Beta strandi165 – 1684Combined sources
Helixi172 – 1743Combined sources
Beta strandi176 – 1794Combined sources
Helixi180 – 1878Combined sources
Beta strandi192 – 1965Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 2076Combined sources
Beta strandi210 – 2178Combined sources
Helixi222 – 2254Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi242 – 2487Combined sources
Helixi249 – 2546Combined sources
Helixi258 – 2636Combined sources
Turni264 – 2674Combined sources
Helixi271 – 28212Combined sources
Helixi288 – 29811Combined sources
Helixi300 – 3023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PPNX-ray2.30A/B1-303[»]
3PPOX-ray2.70A/B1-303[»]
3PPPX-ray2.40A/B1-303[»]
3PPQX-ray1.91A/B1-303[»]
3PPRX-ray2.10A/B1-303[»]
ProteinModelPortaliO32243.
SMRiO32243. Positions 30-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32243.

Family & Domainsi

Sequence similaritiesi

Belongs to the OsmX family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108HQR. Bacteria.
COG1732. LUCA.
HOGENOMiHOG000015716.
InParanoidiO32243.
KOiK05845.
OMAiIGQIDTE.
OrthoDBiEOG6VTK20.
PhylomeDBiO32243.

Family and domain databases

InterProiIPR007210. ABC_Gly_betaine_transp_sub-bd.
[Graphical view]
PfamiPF04069. OpuAC. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O32243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKIKWLGAF ALVFVMLLGG CSLPGLGGAS DDTIKIGAQS MTESEIVANM
60 70 80 90 100
IAQLIEHDTD LNTALVKNLG SNYVQHQAML GGDIDISATR YSGTDLTSTL
110 120 130 140 150
GKEAEKDPKK ALNIVQNEFQ KRFSYKWFDS YGFDNTYAFT VTKKFAEKEH
160 170 180 190 200
INTVSDLKKN ASQYKLGVDN AWLKRKGDGY KGFVSTYGFE FGTTYPMQIG
210 220 230 240 250
LVYDAVKNGK MDAVLAYSTD GRIKAYDLKI LKDDKRFFPP YDCSPVIPEK
260 270 280 290 300
VLKEHPELEG VINKLIGQID TETMQELNYE VDGKLKEPSV VAKEFLEKHH

YFD
Length:303
Mass (Da):33,957
Last modified:January 1, 1998 - v1
Checksum:iBEA28D72D7C7E2F9
GO

Sequence cautioni

The sequence AAB63770.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 542QL → HV in AAB63770 (PubMed:10216873).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009352 Genomic DNA. Translation: AAB63770.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15386.1.
PIRiE69670.
RefSeqiNP_391261.1. NC_000964.3.
WP_003228350.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15386; CAB15386; BSU33810.
GeneIDi936248.
KEGGibsu:BSU33810.
PATRICi18978762. VBIBacSub10457_3544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009352 Genomic DNA. Translation: AAB63770.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15386.1.
PIRiE69670.
RefSeqiNP_391261.1. NC_000964.3.
WP_003228350.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PPNX-ray2.30A/B1-303[»]
3PPOX-ray2.70A/B1-303[»]
3PPPX-ray2.40A/B1-303[»]
3PPQX-ray1.91A/B1-303[»]
3PPRX-ray2.10A/B1-303[»]
ProteinModelPortaliO32243.
SMRiO32243. Positions 30-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018341.

Protein family/group databases

TCDBi3.A.1.12.4. the atp-binding cassette (abc) superfamily.

Proteomic databases

PaxDbiO32243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15386; CAB15386; BSU33810.
GeneIDi936248.
KEGGibsu:BSU33810.
PATRICi18978762. VBIBacSub10457_3544.

Phylogenomic databases

eggNOGiENOG4108HQR. Bacteria.
COG1732. LUCA.
HOGENOMiHOG000015716.
InParanoidiO32243.
KOiK05845.
OMAiIGQIDTE.
OrthoDBiEOG6VTK20.
PhylomeDBiO32243.

Enzyme and pathway databases

BioCyciBSUB:BSU33810-MONOMER.
BRENDAi3.6.3.32. 658.

Miscellaneous databases

EvolutionaryTraceiO32243.

Family and domain databases

InterProiIPR007210. ABC_Gly_betaine_transp_sub-bd.
[Graphical view]
PfamiPF04069. OpuAC. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis."
    Kappes R.M., Kempf B., Kneip S., Boch J., Gade J., Meier-Wagner J., Bremer E.
    Mol. Microbiol. 32:203-216(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: 168 / JH642.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD."
    Kappes R., Kempf B., Bremer E.
    J. Bacteriol. 178:5071-5079(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLYCINE BETAINE TRANSPORT.
    Strain: 168 / JH642.
  4. "Involvement of OpcR, a GbsR-type transcriptional regulator, in negative regulation of two evolutionarily closely related choline uptake genes in Bacillus subtilis."
    Lee C.H., Wu T.Y., Shaw G.C.
    Microbiology 159:2087-2096(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168.

Entry informationi

Entry nameiOPUCC_BACSU
AccessioniPrimary (citable) accession number: O32243
Secondary accession number(s): O31407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.