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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)DescriptionActionsGraphical viewLength
Mutagenesisi12W → M: No changes in biotinylation in E.coli. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00003894942 – 73Biotin/lipoyl attachment proteinAdd BLAST72

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35N6-biotinyllysine; alternatePROSITE-ProRule annotation1 Publication1
Modified residuei35N6-lipoyllysine; alternate1 Publication1

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

173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Beta strandi27 – 33Combined sources7
Beta strandi36 – 41Combined sources6
Beta strandi46 – 53Combined sources8
Beta strandi64 – 68Combined sources5
Helixi69 – 71Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiC0H419.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 69Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 68Biotinyl-binding and/or lipoyl-bindingAdd BLAST67

Sequence similaritiesi

Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4106063. Bacteria.
COG0511. LUCA.
HOGENOMiHOG000020245.
InParanoidiC0H419.
OMAiDSMKMEI.
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)DescriptionActionsGraphical viewLength
Natural varianti4S → I in strain: ATCC 6633. 1
Natural varianti21Q → H in strain: ATCC 6633. 1
Natural varianti47I → T in strain: ATCC 6633. 1
Natural varianti54K → N in strain: ATCC 6633. 1
Natural varianti70N → D in strain: ATCC 6633. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z6HNMR-A2-73[»]
1Z7TNMR-A2-73[»]
2B8FNMR-A2-73[»]
2B8GNMR-A2-73[»]
ProteinModelPortaliC0H419.
SMRiC0H419.
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.
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...

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: November 2, 2016
This is version 47 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.