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Protein

Biotin/lipoyl attachment protein

Gene

yngHB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Keywords - Ligandi

Biotin

Enzyme and pathway databases

BioCyciBSUB:BSU18239-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin/lipoyl attachment protein
Short name:
BLAP
Gene namesi
Name:yngHB
Ordered Locus Names:BSU18239
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121W → M: No changes in biotinylation in E.coli. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 7372Biotin/lipoyl attachment proteinPRO_0000389494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-biotinyllysine; alternatePROSITE-ProRule annotation1 Publication
Modified residuei35 – 351N6-lipoyllysine; alternate1 Publication

Post-translational modificationi

Can be both biotinylated and lipoylated on Lys-35 upon overexpression in E.coli depending on the growth medium; the nature of the modification in situ in B.subtilis is unknown.1 Publication

Proteomic databases

PaxDbiC0H419.

Expressioni

Inductioni

Detected in log-phase B.subtilis cells (at protein level).1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010046.

Structurei

Secondary structure

1
73
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Beta strandi27 – 337Combined sources
Beta strandi36 – 416Combined sources
Beta strandi46 – 538Combined sources
Beta strandi64 – 685Combined sources
Helixi69 – 713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6HNMR-A2-73[»]
1Z7TNMR-A2-73[»]
2B8FNMR-A2-73[»]
2B8GNMR-A2-73[»]
ProteinModelPortaliC0H419.
SMRiC0H419. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiC0H419.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6968Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 6867Biotinyl-binding and/or lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4106063. Bacteria.
COG0511. LUCA.
HOGENOMiHOG000020245.
InParanoidiC0H419.
OMAiDSMKMEI.
OrthoDBiEOG610413.
PhylomeDBiC0H419.

Family and domain databases

InterProiIPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

C0H419-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVSIQMAGN LWKVHVKAGD QIEKGQEVAI LESMKMEIPI VADRSGIVKE
60 70
VKKKEGDFVN EGDVLLELSN STQ
Length:73
Mass (Da):8,041
Last modified:May 5, 2009 - v1
Checksum:i0358FB92D5DBED91
GO

Mass spectrometryi

Molecular mass is 7913 Da from positions 2 - 73. Upon overexpression in E.coli.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41S → I in strain: ATCC 6633.
Natural varianti21 – 211Q → H in strain: ATCC 6633.
Natural varianti47 – 471I → T in strain: ATCC 6633.
Natural varianti54 – 541K → N in strain: ATCC 6633.
Natural varianti70 – 701N → D in strain: ATCC 6633.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184956 Genomic DNA. Translation: AAF08803.1.
AL009126 Genomic DNA. Translation: CAX52627.1.
PIRiT44814.
RefSeqiWP_003245519.1. NZ_JNCM01000035.1.
YP_003097733.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAX52627; CAX52627; BSU18239.
GeneIDi8303012.
KEGGibsu:BSU18239.
PATRICi18975483. VBIBacSub10457_1933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184956 Genomic DNA. Translation: AAF08803.1.
AL009126 Genomic DNA. Translation: CAX52627.1.
PIRiT44814.
RefSeqiWP_003245519.1. NZ_JNCM01000035.1.
YP_003097733.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6HNMR-A2-73[»]
1Z7TNMR-A2-73[»]
2B8FNMR-A2-73[»]
2B8GNMR-A2-73[»]
ProteinModelPortaliC0H419.
SMRiC0H419. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010046.

Proteomic databases

PaxDbiC0H419.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAX52627; CAX52627; BSU18239.
GeneIDi8303012.
KEGGibsu:BSU18239.
PATRICi18975483. VBIBacSub10457_1933.

Phylogenomic databases

eggNOGiENOG4106063. Bacteria.
COG0511. LUCA.
HOGENOMiHOG000020245.
InParanoidiC0H419.
OMAiDSMKMEI.
OrthoDBiEOG610413.
PhylomeDBiC0H419.

Enzyme and pathway databases

BioCyciBSUB:BSU18239-MONOMER.

Miscellaneous databases

EvolutionaryTraceiC0H419.

Family and domain databases

InterProiIPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a multifunctional hybrid between a peptide synthetase, an amino transferase, and a fatty acid synthase."
    Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W., Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F., Vater J.
    Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6633 / PCI 219 / NRS 231.
  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. "Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis."
    Cui G., Nan B., Hu J., Wang Y., Jin C., Xia B.
    J. Biol. Chem. 281:20598-20607(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-73 OF THE APO- AND BIOTINYLATED FORMS, BIOTINYLATION AT LYS-35, LIPOYLATION AT LYS-35, INDUCTION, MASS SPECTROMETRY, MUTAGENESIS OF TRP-12.
    Strain: 168.

Entry informationi

Entry nameiBLAP_BACSU
AccessioniPrimary (citable) accession number: C0H419
Secondary accession number(s): Q9R9I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: May 5, 2009
Last modified: February 17, 2016
This is version 44 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.