Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O31851

- YOJM_BACSU

UniProt

O31851 - YOJM_BACSU

Protein

Superoxide dismutase-like protein YojM

Gene

yojM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi71 – 711Zinc; shared with dimeric partner; structural
    Metal bindingi86 – 861CopperSequence Analysis
    Metal bindingi137 – 1371Zinc; shared with dimeric partner; structural
    Metal bindingi166 – 1661CopperSequence Analysis

    GO - Molecular functioni

    1. copper ion binding Source: RefGenome
    2. superoxide dismutase activity Source: RefGenome
    3. zinc ion binding Source: RefGenome

    GO - Biological processi

    1. removal of superoxide radicals Source: RefGenome

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU19400-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase-like protein YojM
    Gene namesi
    Name:yojM
    Ordered Locus Names:BSU19400
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU19400.

    Subcellular locationi

    Cell membrane PROSITE-ProRule annotation; Lipid-anchor PROSITE-ProRule annotation

    GO - Cellular componenti

    1. periplasmic space Source: RefGenome
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881Y → H: Leads to copper binding and enzyme activity; when associated with H-104. 1 Publication
    Mutagenesisi104 – 1041P → H: Leads to copper binding and enzyme activity; when associated with H-88. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717PROSITE-ProRule annotationAdd
    BLAST
    Chaini18 – 196179Superoxide dismutase-like protein YojMPRO_0000032842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi18 – 181N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi18 – 181S-diacylglycerol cysteinePROSITE-ProRule annotation
    Disulfide bondi93 ↔ 186

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiO31851.

    Interactioni

    Subunit structurei

    Monomer, and homodimer. Largely unstructured monomer in solution. Well-ordered homodimer in the crystal.2 Publications

    Protein-protein interaction databases

    IntActiO31851. 19 interactions.
    STRINGi224308.BSU19400.

    Structurei

    Secondary structure

    1
    196
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 498
    Turni50 – 523
    Beta strandi54 – 629
    Beta strandi64 – 7411
    Beta strandi85 – 906
    Turni91 – 933
    Turni95 – 973
    Helixi99 – 1013
    Beta strandi124 – 1296
    Beta strandi136 – 1427
    Beta strandi149 – 1524
    Beta strandi154 – 1574
    Beta strandi161 – 1688
    Beta strandi172 – 1743
    Turni175 – 1795
    Beta strandi182 – 1898

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00257.
    ProteinModelPortaliO31851.
    SMRiO31851. Positions 40-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO31851.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2032.
    HOGENOMiHOG000263448.
    KOiK04565.
    OMAiHANSDDY.
    OrthoDBiEOG6K13RS.
    PhylomeDBiO31851.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O31851-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHRLLLLMML TALGVAGCGQ KKPPDPPNRV PEKKVVETSA FGHHVQLVNR    50
    EGKAVGFIEI KESDDEGLDI HISANSLRPG ASLGFHIYEK GSCVRPDFES 100
    AGGPFNPLNK EHGFNNPMGH HAGDLPNLEV GADGKVDVIM NAPDTSLKKG 150
    SKLNILDEDG SAFIIHEQAD DYLTNPSGNS GARIVCGALL GNNEKQ 196
    Length:196
    Mass (Da):20,953
    Last modified:January 1, 1998 - v1
    Checksum:i7C00301A62188306
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026147 Genomic DNA. Translation: AAC17861.1.
    AL009126 Genomic DNA. Translation: CAB13832.1.
    PIRiB69907.
    RefSeqiNP_389822.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13832; CAB13832; BSU19400.
    GeneIDi939502.
    KEGGibsu:BSU19400.
    PATRICi18975731. VBIBacSub10457_2056.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026147 Genomic DNA. Translation: AAC17861.1 .
    AL009126 Genomic DNA. Translation: CAB13832.1 .
    PIRi B69907.
    RefSeqi NP_389822.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S4I X-ray 1.80 A/B/C/D 22-196 [» ]
    1U3N NMR - A 35-196 [» ]
    1XTL X-ray 2.00 A/B/C/D 22-196 [» ]
    1XTM X-ray 1.60 A/B 22-196 [» ]
    DisProti DP00257.
    ProteinModelPortali O31851.
    SMRi O31851. Positions 40-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O31851. 19 interactions.
    STRINGi 224308.BSU19400.

    Proteomic databases

    PaxDbi O31851.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13832 ; CAB13832 ; BSU19400 .
    GeneIDi 939502.
    KEGGi bsu:BSU19400.
    PATRICi 18975731. VBIBacSub10457_2056.

    Organism-specific databases

    GenoListi BSU19400.

    Phylogenomic databases

    eggNOGi COG2032.
    HOGENOMi HOG000263448.
    KOi K04565.
    OMAi HANSDDY.
    OrthoDBi EOG6K13RS.
    PhylomeDBi O31851.

    Enzyme and pathway databases

    BioCyci BSUB:BSU19400-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O31851.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiYOJM_BACSU
    AccessioniPrimary (citable) accession number: O31851
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 113 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

    External Data

    Dasty 3