Skip Header

Contribute Send feedback
Read comments (?) or add your own

O31851 (YOJM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase-like protein YojM
Gene names
Name:yojM
Ordered Locus Names:BSU19400
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per homodimer. The zinc ion is bound between 2 subunits and mediates dimerization.

Subunit structure

Monomer, and homodimer. Largely unstructured monomer in solution. Well-ordered homodimer in the crystal. Ref.4

Subcellular location

Cell membrane; Lipid-anchor Potential.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 196179Superoxide dismutase-like protein YojM
PRO_0000032842

Sites

Metal binding711Zinc; shared with dimeric partner; structural
Metal binding861Copper Potential
Metal binding1371Zinc; shared with dimeric partner; structural
Metal binding1661Copper Potential

Amino acid modifications

Lipidation181N-palmitoyl cysteine Potential
Lipidation181S-diacylglycerol cysteine Potential
Disulfide bond93 ↔ 186

Experimental info

Mutagenesis881Y → H: Leads to copper binding and enzyme activity; when associated with H-104. Ref.3
Mutagenesis1041P → H: Leads to copper binding and enzyme activity; when associated with H-88. Ref.3

Secondary structure

1 .............................. 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O31851 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7C00301A62188306

FASTA19620,953
        10         20         30         40         50         60 
MHRLLLLMML TALGVAGCGQ KKPPDPPNRV PEKKVVETSA FGHHVQLVNR EGKAVGFIEI 

        70         80         90        100        110        120 
KESDDEGLDI HISANSLRPG ASLGFHIYEK GSCVRPDFES AGGPFNPLNK EHGFNNPMGH 

       130        140        150        160        170        180 
HAGDLPNLEV GADGKVDVIM NAPDTSLKKG SKLNILDEDG SAFIIHEQAD DYLTNPSGNS 

       190 
GARIVCGALL GNNEKQ

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis 168 chromosome region between the sspC and odhA loci (184 degrees-180 degrees)."
Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D., Park S.-H.
DNA Res. 5:195-201(1998) [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.
[3]"From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis."
Banci L., Benvenuti M., Bertini I., Cabelli D.E., Calderone V., Fantoni A., Mangani S., Migliardi M., Viezzoli M.S.
J. Am. Chem. Soc. 127:13287-13292(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-196 OF MUTANT HIS-88/HIS-104 IN COMPLEX WITH COPPER AND ZINC IONS, MUTAGENESIS OF TYR-88 AND PRO-104.
[4]"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal."
Banci L., Bertini I., Calderone V., Cramaro F., Del Conte R., Fantoni A., Mangani S., Quattrone A., Viezzoli M.S.
Proc. Natl. Acad. Sci. U.S.A. 102:7541-7546(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-196 IN COMPLEX WITH ZINC IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF026147 Genomic DNA. Translation: AAC17861.1.
AL009126 Genomic DNA. Translation: CAB13832.1.
PIRB69907.
RefSeqNP_389822.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4IX-ray1.80A/B/C/D22-196[»]
1U3NNMR-A35-196[»]
1XTLX-ray2.00A/B/C/D22-196[»]
1XTMX-ray1.60A/B22-196[»]
DisProtDP00257.
ProteinModelPortalO31851.
SMRO31851. Positions 40-191.
ModBaseSearch...

Protein-protein interaction databases

IntActO31851. 19 interactions.
STRING224308.BSU19400.

Proteomic databases

PaxDbO31851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13832; CAB13832; BSU19400.
GeneID939502.
KEGGbsu:BSU19400.
PATRIC18975731. VBIBacSub10457_2056.

Organism-specific databases

GenoListBSU19400.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263448.
KOK04565.
OMADVIMNAP.
ProtClustDBCLSK887425.

Enzyme and pathway databases

BioCycBSUB:BSU19400-MONOMER.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00087. SOD_CU_ZN_1. False negative.
PS00332. SOD_CU_ZN_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO31851.

Entry information

Entry nameYOJM_BACSU
AccessionPrimary (citable) accession number: O31851
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 105 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents