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O34518 (AMYC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative ABC transporter permease protein AmyC
Gene names
Name:amyC
Ordered Locus Names:BSU30290
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane.

Subunit structure

The complex is composed of two transmembrane proteins (AmyC and AmyD), a solute-binding protein (MsmE) and an unknown ATP-binding protein Potential.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the binding-protein-dependent transport system permease family.

Contains 1 ABC transmembrane type-1 domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276Putative ABC transporter permease protein AmyC
PRO_0000387964

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane74 – 9421Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane139 – 15921Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane240 – 26021Helical; Potential
Domain69 – 261193ABC transmembrane type-1

Sequences

Sequence LengthMass (Da)Tools
O34518 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: AC3B77CEA23C8DC8

FASTA27630,375
        10         20         30         40         50         60 
MRAARTKSMR IITLLAAIVA CAHFIPFYIL LTTSLKAKGD YSSKWIFPAD ISFHNFSEAW 

        70         80         90        100        110        120 
ERASLGNSFI NTMIITGFSA LLLIIFGSLA AYPLARRETK LNKAVFALLI SIMIIPPLTS 

       130        140        150        160        170        180 
MVPLYRMVVD AGMVNTHAIA IFINTAAYMP LTVFLYSGFI RSTIPKELVE AARIDGAGML 

       190        200        210        220        230        240 
KIFFTIVFPL LKPITATICI ISCVFIWNDY QFAIFFLQDQ KVQTLTVAMA GFFGENANNL 

       250        260        270 
HLVAAAALMA MLPMVVLFLA LQKYFIAGLS SGAVKG

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF008220 Genomic DNA. Translation: AAC00384.1.
AL009126 Genomic DNA. Translation: CAB15007.1.
PIRD69585.
RefSeqNP_390907.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34518.
SMRO34518. Positions 3-276.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU30290.

Proteomic databases

PaxDbO34518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15007; CAB15007; BSU30290.
GeneID935927.
KEGGbsu:BSU30290.
PATRIC18977960. VBIBacSub10457_3168.

Organism-specific databases

GenoListBSU30290. [Micado]

Phylogenomic databases

eggNOGCOG0395.
HOGENOMHOG000220525.
KOK10119.
OMAIWNDYQF.
ProtClustDBCLSK873254.

Enzyme and pathway databases

BioCycBSUB:BSU30290-MONOMER.

Family and domain databases

InterProIPR000515. BPD_transp.
[Graphical view]
PfamPF00528. BPD_transp_1. 1 hit.
[Graphical view]
PROSITEPS50928. ABC_TM1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYC_BACSU
AccessionPrimary (citable) accession number: O34518
Secondary accession number(s): Q795Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

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