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P51834

- SMC_BACSU

UniProt

P51834 - SMC_BACSU

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Protein

Chromosome partition protein Smc

Gene

smc

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

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

GO - Biological processi

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

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-HAMAP
Complete GO annotation...

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 – 149Combined sources
Beta strandi24 – 307Combined sources
Helixi39 – 4810Combined sources
Beta strandi83 – 897Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi112 – 1143Combined sources
Helixi122 – 1254Combined sources
Helixi126 – 1283Combined sources
Beta strandi139 – 1424Combined sources
Helixi143 – 1519Combined sources
Helixi154 – 16411Combined sources
Helixi168 – 19730Combined sources
Helixi996 – 105257Combined sources
Beta strandi1056 – 10594Combined sources
Beta strandi1062 – 10665Combined sources
Helixi1067 – 10693Combined sources
Beta strandi1074 – 10774Combined sources
Beta strandi1079 – 10813Combined sources
Beta strandi1083 – 10897Combined sources
Helixi1093 – 110816Combined sources
Beta strandi1114 – 11185Combined sources
Turni1119 – 11224Combined sources
Helixi1126 – 113712Combined sources
Beta strandi1139 – 11424Combined sources
Beta strandi1144 – 11474Combined sources
Helixi1151 – 11566Combined sources
Beta strandi1160 – 11645Combined sources
Beta strandi1171 – 11744Combined sources

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.
InParanoidiP51834.
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

        10         20         30         40         50
MFLKRLDVIG FKSFAERISV DFVKGVTAVV GPNGSGKSNI TDAIRWVLGE
60 70 80 90 100
QSARSLRGGK MEDIIFAGSD SRKRLNLAEV TLTLDNDDHF LPIDFHEVSV
110 120 130 140 150
TRRVYRSGES EFLINNQPCR LKDIIDLFMD SGLGKEAFSI ISQGKVEEIL
160 170 180 190 200
SSKAEDRRSI FEEAAGVLKY KTRKKKAENK LFETQDNLNR VEDILHELEG
210 220 230 240 250
QVEPLKIQAS IAKDYLEKKK ELEHVEIALT AYDIEELHGK WSTLKEKVQM
260 270 280 290 300
AKEEELAESS AISAKEAKIE DTRDKIQALD ESVDELQQVL LVTSEELEKL
310 320 330 340 350
EGRKEVLKER KKNAVQNQEQ LEEAIVQFQQ KETVLKEELS KQEAVFETLQ
360 370 380 390 400
AEVKQLRAQV KEKQQALSLH NENVEEKIEQ LKSDYFELLN SQASIRNELQ
410 420 430 440 450
LLDDQMSQSA VTLQRLADNN EKHLQERHDI SARKAACETE FARIEQEIHS
460 470 480 490 500
QVGAYRDMQT KYEQKKRQYE KNESALYQAY QYVQQARSKK DMLETMQGDF
510 520 530 540 550
SGFYQGVKEV LKAKERLGGI RGAVLELIST EQKYETAIEI ALGASAQHVV
560 570 580 590 600
TDDEQSARKA IQYLKQNSFG RATFLPLSVI RDRQLQSRDA ETAARHSSFL
610 620 630 640 650
GVASELVTFD PAYRSVIQNL LGTVLITEDL KGANELAKLL GHRYRIVTLE
660 670 680 690 700
GDVVNPGGSM TGGAVKKKNN SLLGRSRELE DVTKRLAEME EKTALLEQEV
710 720 730 740 750
KTLKHSIQDM EKKLADLRET GEGLRLKQQD VKGQLYELQV AEKNINTHLE
760 770 780 790 800
LYDQEKSALS ESDEERKVRK RKLEEELSAV SEKMKQLEED IDRLTKQKQT
810 820 830 840 850
QSSTKESLSN ELTELKIAAA KKEQACKGEE DNLARLKKEL TETELALKEA
860 870 880 890 900
KEDLSFLTSE MSSSTSGEEK LEEAAKHKLN DKTKTIELIA LRRDQRIKLQ
910 920 930 940 950
HGLDTYEREL KEMKRLYKQK TTLLKDEEVK LGRMEVELDN LLQYLREEYS
960 970 980 990 1000
LSFEGAKEKY QLETDPEEAR KRVKLIKLAI EELGTVNLGS IDEFERVNER
1010 1020 1030 1040 1050
YKFLSEQKED LTEAKNTLFQ VIEEMDEEMT KRFNDTFVQI RSHFDQVFRS
1060 1070 1080 1090 1100
LFGGGRAELR LTDPNDLLHS GVEIIAQPPG KKLQNLNLLS GGERALTAIA
1110 1120 1130 1140 1150
LLFSILKVRP VPFCVLDEVE AALDEANVFR FAQYLKKYSS DTQFIVITHR
1160 1170 1180
KGTMEEADVL YGVTMQESGV SKVISVKLEE TKEFVQ
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.
InParanoidi P51834.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 109 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