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Protein

Chromosome partition protein Smc

Gene

smc

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

Functioni

Required for chromosome condensation and partitioning.UniRule annotation2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

  • Note: Probably associated with the nucleoid.

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001190281 – 1186Chromosome partition protein SmcAdd BLAST1186

Proteomic databases

PaxDbiP51834.
PRIDEiP51834.

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 interactors.
STRINGi224308.Bsubs1_010100008791.

Structurei

Secondary structure

11186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 14Combined sources9
Beta strandi24 – 30Combined sources7
Helixi39 – 48Combined sources10
Beta strandi83 – 89Combined sources7
Beta strandi100 – 107Combined sources8
Beta strandi112 – 114Combined sources3
Helixi122 – 125Combined sources4
Helixi126 – 128Combined sources3
Beta strandi139 – 142Combined sources4
Helixi143 – 151Combined sources9
Helixi154 – 164Combined sources11
Helixi168 – 197Combined sources30
Helixi996 – 1052Combined sources57
Beta strandi1056 – 1059Combined sources4
Beta strandi1062 – 1066Combined sources5
Helixi1067 – 1069Combined sources3
Beta strandi1074 – 1077Combined sources4
Beta strandi1079 – 1081Combined sources3
Beta strandi1083 – 1089Combined sources7
Helixi1093 – 1108Combined sources16
Beta strandi1114 – 1118Combined sources5
Turni1119 – 1122Combined sources4
Helixi1126 – 1137Combined sources12
Beta strandi1139 – 1142Combined sources4
Beta strandi1144 – 1147Combined sources4
Helixi1151 – 1156Combined sources6
Beta strandi1160 – 1164Combined sources5
Beta strandi1171 – 1174Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGXX-ray3.40A/B1-219[»]
A/B983-1186[»]
ProteinModelPortaliP51834.
SMRiP51834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili167 – 206UniRule annotationAdd BLAST40
Coiled coili259 – 481UniRule annotationAdd BLAST223
Coiled coili672 – 864UniRule annotationAdd BLAST193
Coiled coili893 – 943UniRule annotationAdd BLAST51
Coiled coili990 – 1029UniRule annotationAdd BLAST40

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

eggNOGiENOG4105CDB. Bacteria.
COG1196. LUCA.
HOGENOMiHOG000036392.
InParanoidiP51834.
KOiK03529.
OMAiLHFKQQK.
PhylomeDBiP51834.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01894. Smc_prok. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti50E → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti162E → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti175K → E in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti178E → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti192E → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti228A → P in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti264A → P in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti271D → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti309E → D in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti336 – 342KEELSKQ → TRRAFEA in BAA10977 (PubMed:8654983).Curated7
Sequence conflicti365Q → H in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti438E → K in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti444I → F in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti475A → P in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti494E → D in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti515E → D in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti542L → V in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti546A → P in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti586 – 600QSRDA…HSSFL → SKPLRGNSGPAFIISF in BAA10977 (PubMed:8654983).CuratedAdd BLAST15
Sequence conflicti623 – 631TVLITEDLK → NRSDYRGLKG in BAA10977 (PubMed:8654983).Curated9
Sequence conflicti664A → S in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti676S → T in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti680E → G in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti694A → S in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti701K → Q in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti726L → V in BAA10977 (PubMed:8654983).Curated1
Sequence conflicti738 – 740LQV → PQF in BAA10977 (PubMed:8654983).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003232028.1. NZ_JNCM01000035.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003232028.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGXX-ray3.40A/B1-219[»]
A/B983-1186[»]
ProteinModelPortaliP51834.
SMRiP51834.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-52199N.
IntActiP51834. 22 interactors.
STRINGi224308.Bsubs1_010100008791.

Proteomic databases

PaxDbiP51834.
PRIDEiP51834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CDB. Bacteria.
COG1196. LUCA.
HOGENOMiHOG000036392.
InParanoidiP51834.
KOiK03529.
OMAiLHFKQQK.
PhylomeDBiP51834.

Enzyme and pathway databases

BioCyciBSUB:BSU15940-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01894. Smc_prok. 1 hit.
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.
ProtoNetiSearch...

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: November 2, 2016
This is version 121 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

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.