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P35154

- SCPA_BACSU

UniProt

P35154 - SCPA_BACSU

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Protein

Segregation and condensation protein A

Gene
scpA, ypuG, BSU23220
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.UniRule annotation

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. chromosome segregation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition

Enzyme and pathway databases

BioCyciBSUB:BSU23220-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Segregation and condensation protein A
Gene namesi
Name:scpA
Synonyms:ypuG
Ordered Locus Names:BSU23220
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU23220. [Micado]

Subcellular locationi

Cytoplasm
Note: Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Segregation and condensation protein AUniRule annotationPRO_0000211080Add
BLAST

Proteomic databases

PaxDbiP35154.

Interactioni

Subunit structurei

Component of a cohesin-like complex composed of ScpA, ScpB and the Smc homodimer, in which ScpA and ScpB bind to the head domain of Smc. The presence of the three proteins is required for the association of the complex with DNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
scpBP351553EBI-2121359,EBI-2121445
smcP518346EBI-2121359,EBI-2121372

Protein-protein interaction databases

DIPiDIP-52200N.
IntActiP35154. 15 interactions.
STRINGi224308.BSU23220.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2916
Beta strandi31 – 344
Helixi39 – 7335

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGXX-ray3.40C/Z1-86[»]
ProteinModelPortaliP35154.

Family & Domainsi

Sequence similaritiesi

Belongs to the ScpA family.

Phylogenomic databases

eggNOGiCOG1354.
HOGENOMiHOG000242824.
KOiK05896.
OMAiNILDIPM.
OrthoDBiEOG6CZQPX.
PhylomeDBiP35154.

Family and domain databases

HAMAPiMF_01805. ScpA.
InterProiIPR003768. ScpA.
[Graphical view]
PfamiPF02616. ScpA_ScpB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35154-1 [UniParc]FASTAAdd to Basket

« Hide

MEEYQVKIDT FEGPLDLLLH LINRLEIDIY DIPVAKITEQ YLLYVHTMRV    50
LELDIASEYL VMAATLLSIK SRMLLPKQEE ELFEDELLEE EDPREELIEK 100
LIEYRKYKDA AKDLKEREEE RQKSFTKPPS DLSEYAKEVK QSEQKLSVTV 150
YDMIGAFQKV LKRKKINRPM ETTITRQDIP IEARMNEIVH SLKSRGTRIN 200
FMDLFPYEQK EHLVVTFLAV LELMKNQLVL IEQEHNFSDI YITGSESIHG 250
A 251
Length:251
Mass (Da):29,612
Last modified:February 1, 1994 - v1
Checksum:i9FE03F117D2919A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09228 Genomic DNA. Translation: AAA67487.1.
AL009126 Genomic DNA. Translation: CAB14254.1.
PIRiS45549.
RefSeqiNP_390203.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14254; CAB14254; BSU23220.
GeneIDi938950.
KEGGibsu:BSU23220.
PATRICi18976461. VBIBacSub10457_2421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09228 Genomic DNA. Translation: AAA67487.1 .
AL009126 Genomic DNA. Translation: CAB14254.1 .
PIRi S45549.
RefSeqi NP_390203.1. 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 C/Z 1-86 [» ]
ProteinModelPortali P35154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-52200N.
IntActi P35154. 15 interactions.
STRINGi 224308.BSU23220.

Proteomic databases

PaxDbi P35154.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14254 ; CAB14254 ; BSU23220 .
GeneIDi 938950.
KEGGi bsu:BSU23220.
PATRICi 18976461. VBIBacSub10457_2421.

Organism-specific databases

GenoListi BSU23220. [Micado ]

Phylogenomic databases

eggNOGi COG1354.
HOGENOMi HOG000242824.
KOi K05896.
OMAi NILDIPM.
OrthoDBi EOG6CZQPX.
PhylomeDBi P35154.

Enzyme and pathway databases

BioCyci BSUB:BSU23220-MONOMER.

Family and domain databases

HAMAPi MF_01805. ScpA.
InterProi IPR003768. ScpA.
[Graphical view ]
Pfami PF02616. ScpA_ScpB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data."
    Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.
    Mol. Microbiol. 10:385-395(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  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. "Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein."
    Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L.
    EMBO J. 21:3108-3118(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCPB AND SMC.
  4. "Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB."
    Soppa J., Kobayashi K., Noirot-Gros M.-F., Oesterhelt D., Ehrlich S.D., Dervyn E., Ogasawara N., Moriya S.
    Mol. Microbiol. 45:59-71(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH SCPB.
  5. "A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure."
    Volkov A., Mascarenhas J., Andrei-Selmer C., Ulrich H.D., Graumann P.L.
    Mol. Cell. Biol. 23:5638-5650(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, HOMODIMERIZATION, INTERACTION WITH SMC AND SCPB.

Entry informationi

Entry nameiSCPA_BACSU
AccessioniPrimary (citable) accession number: P35154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 94 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

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