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P51834

- SMC_BACSU

UniProt

P51834 - SMC_BACSU

Protein

Chromosome partition protein Smc

Gene

smc

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Required for chromosome condensation and partitioning.2 PublicationsUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 398ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. DNA binding Source: UniProtKB-HAMAP
    3. identical protein binding Source: IntAct
    4. protein binding Source: IntAct

    GO - Biological processi

    1. chromosome condensation Source: InterPro
    2. DNA replication Source: UniProtKB-HAMAP
    3. sister chromatid cohesion Source: InterPro

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU15940-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromosome partition protein SmcUniRule annotation
    Gene namesi
    Name:smcUniRule annotation
    Synonyms:ylqA
    Ordered Locus Names:BSU15940
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15940. [Micado]

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation
    Note: Probably associated with the nucleoid.

    GO - Cellular componenti

    1. chromosome Source: InterPro
    2. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutants produce anucleate cells and show defects in nucleoid structure and in chromosome partitioning.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11861186Chromosome partition protein SmcPRO_0000119028Add
    BLAST

    Proteomic databases

    PaxDbiP51834.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-2121372,EBI-2121372
    scpAP351546EBI-2121372,EBI-2121359
    scpBP351552EBI-2121372,EBI-2121445

    Protein-protein interaction databases

    DIPiDIP-52199N.
    IntActiP51834. 22 interactions.
    STRINGi224308.BSU15940.

    Structurei

    Secondary structure

    1
    1186
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 149
    Beta strandi24 – 307
    Helixi39 – 4810
    Beta strandi83 – 897
    Beta strandi100 – 1078
    Beta strandi112 – 1143
    Helixi122 – 1254
    Helixi126 – 1283
    Beta strandi139 – 1424
    Helixi143 – 1519
    Helixi154 – 16411
    Helixi168 – 19730
    Helixi996 – 105257
    Beta strandi1056 – 10594
    Beta strandi1062 – 10665
    Helixi1067 – 10693
    Beta strandi1074 – 10774
    Beta strandi1079 – 10813
    Beta strandi1083 – 10897
    Helixi1093 – 110816
    Beta strandi1114 – 11185
    Turni1119 – 11224
    Helixi1126 – 113712
    Beta strandi1139 – 11424
    Beta strandi1144 – 11474
    Helixi1151 – 11566
    Beta strandi1160 – 11645
    Beta strandi1171 – 11744

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZGXX-ray3.40A/B1-219[»]
    A/B983-1186[»]
    ProteinModelPortaliP51834.
    SMRiP51834. Positions 1-197, 485-685, 1029-1186.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili167 – 20640UniRule annotationAdd
    BLAST
    Coiled coili259 – 481223UniRule annotationAdd
    BLAST
    Coiled coili672 – 864193UniRule annotationAdd
    BLAST
    Coiled coili893 – 94351UniRule annotationAdd
    BLAST
    Coiled coili990 – 102940UniRule annotationAdd
    BLAST

    Domaini

    Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures.UniRule annotation

    Sequence similaritiesi

    Belongs to the SMC family.UniRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1196.
    HOGENOMiHOG000036392.
    KOiK03529.
    OrthoDBiEOG6WQD34.
    PhylomeDBiP51834.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_01894. Smc_prok.
    InterProiIPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    IPR011890. SMC_prok.
    [Graphical view]
    PfamiPF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005719. SMC. 1 hit.
    SMARTiSM00968. SMC_hinge. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF75553. SSF75553. 1 hit.
    TIGRFAMsiTIGR02168. SMC_prok_B. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P51834-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLKRLDVIG FKSFAERISV DFVKGVTAVV GPNGSGKSNI TDAIRWVLGE     50
    QSARSLRGGK MEDIIFAGSD SRKRLNLAEV TLTLDNDDHF LPIDFHEVSV 100
    TRRVYRSGES EFLINNQPCR LKDIIDLFMD SGLGKEAFSI ISQGKVEEIL 150
    SSKAEDRRSI FEEAAGVLKY KTRKKKAENK LFETQDNLNR VEDILHELEG 200
    QVEPLKIQAS IAKDYLEKKK ELEHVEIALT AYDIEELHGK WSTLKEKVQM 250
    AKEEELAESS AISAKEAKIE DTRDKIQALD ESVDELQQVL LVTSEELEKL 300
    EGRKEVLKER KKNAVQNQEQ LEEAIVQFQQ KETVLKEELS KQEAVFETLQ 350
    AEVKQLRAQV KEKQQALSLH NENVEEKIEQ LKSDYFELLN SQASIRNELQ 400
    LLDDQMSQSA VTLQRLADNN EKHLQERHDI SARKAACETE FARIEQEIHS 450
    QVGAYRDMQT KYEQKKRQYE KNESALYQAY QYVQQARSKK DMLETMQGDF 500
    SGFYQGVKEV LKAKERLGGI RGAVLELIST EQKYETAIEI ALGASAQHVV 550
    TDDEQSARKA IQYLKQNSFG RATFLPLSVI RDRQLQSRDA ETAARHSSFL 600
    GVASELVTFD PAYRSVIQNL LGTVLITEDL KGANELAKLL GHRYRIVTLE 650
    GDVVNPGGSM TGGAVKKKNN SLLGRSRELE DVTKRLAEME EKTALLEQEV 700
    KTLKHSIQDM EKKLADLRET GEGLRLKQQD VKGQLYELQV AEKNINTHLE 750
    LYDQEKSALS ESDEERKVRK RKLEEELSAV SEKMKQLEED IDRLTKQKQT 800
    QSSTKESLSN ELTELKIAAA KKEQACKGEE DNLARLKKEL TETELALKEA 850
    KEDLSFLTSE MSSSTSGEEK LEEAAKHKLN DKTKTIELIA LRRDQRIKLQ 900
    HGLDTYEREL KEMKRLYKQK TTLLKDEEVK LGRMEVELDN LLQYLREEYS 950
    LSFEGAKEKY QLETDPEEAR KRVKLIKLAI EELGTVNLGS IDEFERVNER 1000
    YKFLSEQKED LTEAKNTLFQ VIEEMDEEMT KRFNDTFVQI RSHFDQVFRS 1050
    LFGGGRAELR LTDPNDLLHS GVEIIAQPPG KKLQNLNLLS GGERALTAIA 1100
    LLFSILKVRP VPFCVLDEVE AALDEANVFR FAQYLKKYSS DTQFIVITHR 1150
    KGTMEEADVL YGVTMQESGV SKVISVKLEE TKEFVQ 1186
    Length:1,186
    Mass (Da):135,513
    Last modified:June 16, 2009 - v3
    Checksum:iACC5D1A170453212
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501E → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti162 – 1621E → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti175 – 1751K → E in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti178 – 1781E → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti192 – 1921E → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti228 – 2281A → P in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti264 – 2641A → P in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti271 – 2711D → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti309 – 3091E → D in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti336 – 3427KEELSKQ → TRRAFEA in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti365 – 3651Q → H in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti438 – 4381E → K in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti444 – 4441I → F in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti475 – 4751A → P in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti494 – 4941E → D in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti515 – 5151E → D in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti542 – 5421L → V in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti546 – 5461A → P in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti586 – 60015QSRDA…HSSFL → SKPLRGNSGPAFIISF in BAA10977. (PubMed:8654983)CuratedAdd
    BLAST
    Sequence conflicti623 – 6319TVLITEDLK → NRSDYRGLKG in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti664 – 6641A → S in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti676 – 6761S → T in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti680 – 6801E → G in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti694 – 6941A → S in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti701 – 7011K → Q in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti726 – 7261L → V in BAA10977. (PubMed:8654983)Curated
    Sequence conflicti738 – 7403LQV → PQF in BAA10977. (PubMed:8654983)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64116 Genomic DNA. Translation: BAA10977.1.
    AL009126 Genomic DNA. Translation: CAB13467.2.
    D49781 Genomic DNA. Translation: BAA08615.1.
    PIRiG69708.
    RefSeqiNP_389476.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13467; CAB13467; BSU15940.
    GeneIDi938085.
    KEGGibsu:BSU15940.
    PATRICi18974993. VBIBacSub10457_1688.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64116 Genomic DNA. Translation: BAA10977.1 .
    AL009126 Genomic DNA. Translation: CAB13467.2 .
    D49781 Genomic DNA. Translation: BAA08615.1 .
    PIRi G69708.
    RefSeqi NP_389476.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZGX X-ray 3.40 A/B 1-219 [» ]
    A/B 983-1186 [» ]
    ProteinModelPortali P51834.
    SMRi P51834. Positions 1-197, 485-685, 1029-1186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-52199N.
    IntActi P51834. 22 interactions.
    STRINGi 224308.BSU15940.

    Proteomic databases

    PaxDbi P51834.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13467 ; CAB13467 ; BSU15940 .
    GeneIDi 938085.
    KEGGi bsu:BSU15940.
    PATRICi 18974993. VBIBacSub10457_1688.

    Organism-specific databases

    GenoListi BSU15940. [Micado ]

    Phylogenomic databases

    eggNOGi COG1196.
    HOGENOMi HOG000036392.
    KOi K03529.
    OrthoDBi EOG6WQD34.
    PhylomeDBi P51834.

    Enzyme and pathway databases

    BioCyci BSUB:BSU15940-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_01894. Smc_prok.
    InterProi IPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    IPR011890. SMC_prok.
    [Graphical view ]
    Pfami PF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005719. SMC. 1 hit.
    SMARTi SM00968. SMC_hinge. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF75553. SSF75553. 1 hit.
    TIGRFAMsi TIGR02168. SMC_prok_B. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation."
      Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.
      Gene 172:17-24(1996) [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 a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 236 AND 284.
    4. "srb: a Bacillus subtilis gene encoding a homologue of the alpha-subunit of the mammalian signal recognition particle receptor."
      Oguro A., Kakeshita H., Honda K., Takamatsu H., Nakamura K., Yamane K.
      DNA Res. 2:95-100(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1171-1186.
      Strain: 168.
    5. "Characterization of a prokaryotic SMC protein involved in chromosome partitioning."
      Britton R.A., Lin D.C., Grossman A.D.
      Genes Dev. 12:1254-1259(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
      Strain: 168 / JH642.
    6. "A Bacillus subtilis gene-encoding protein homologous to eukaryotic SMC motor protein is necessary for chromosome partition."
      Moriya S., Tsujikawa E., Hassan A.K., Asai K., Kodama T., Ogasawara N.
      Mol. Microbiol. 29:179-187(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      Strain: 168.

    Entry informationi

    Entry nameiSMC_BACSU
    AccessioniPrimary (citable) accession number: P51834
    Secondary accession number(s): O31735
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 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