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Protein

Stage II sporulation protein Q

Gene

spoIIQ

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

Functioni

Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.10 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU36550-MONOMER.

Protein family/group databases

TCDBi1.A.34.1.1. 1.a.34 the bacillus gap junction-like channel-forming complex (gj-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Stage II sporulation protein Q
Gene namesi
Name:spoIIQ
Synonyms:ywnI
Ordered Locus Names:BSU36550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endospore-forming forespore Source: CACAO
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Stage II sporulation protein QPRO_0000360550Add
BLAST

Proteomic databases

PaxDbiP71044.

Expressioni

Developmental stagei

Specifically expressed in the forespore under the control of the sigma-K factor.2 Publications

Interactioni

Subunit structurei

Interacts with SpoIIIAH and SpoIIE.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
spoIIIAHP497854EBI-6413220,EBI-6413215

Protein-protein interaction databases

DIPiDIP-60029N.
IntActiP71044. 1 interaction.
STRINGi224308.Bsubs1_010100019756.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 793Combined sources
Beta strandi82 – 854Combined sources
Helixi86 – 883Combined sources
Beta strandi89 – 935Combined sources
Beta strandi98 – 1003Combined sources
Helixi102 – 1076Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi140 – 1489Combined sources
Turni149 – 1513Combined sources
Beta strandi152 – 1587Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 17412Combined sources
Beta strandi186 – 1894Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2099Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 2183Combined sources
Helixi224 – 2274Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TUFX-ray2.26B43-283[»]
3UZ0X-ray2.82B/D73-220[»]
ProteinModelPortaliP71044.
SMRiP71044. Positions 117-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105FRN. Bacteria.
COG0739. LUCA.
HOGENOMiHOG000099586.
InParanoidiP71044.
KOiK06386.
OMAiTAVLWYQ.
OrthoDBiEOG64JFMH.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.

Sequencei

Sequence statusi: Complete.

P71044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREEEKKTSQ VKKLQQFFRK RWVFPAIYLV SAAVILTAVL WYQSVSNDEV
60 70 80 90 100
KDQLADNGGN SAYDNNDDAV EVGKSMENVA MPVVDSENVS VVKKFYETDA
110 120 130 140 150
AKEEKEAALV TYNNTYSLSK GIDLAEKDGK DFDVSASLSG TVVKAEKDPV
160 170 180 190 200
LGYVVEVEHA DGLSTVYQSL SEVSVEQGDK VKQNQVIGKS GKNLYSEDSG
210 220 230 240 250
NHVHFEIRKD GVAMNPLNFM DKPVSSIEKA ATQETEESIQ QSSEKKDGST
260 270 280
EKGTEEKSGE KKDDSTDKSG SKESSTTEDT EQS
Length:283
Mass (Da):31,113
Last modified:February 1, 1997 - v1
Checksum:iE913200AF563C98C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69855.1.
AL009126 Genomic DNA. Translation: CAB15672.1.
PIRiB69713.
RefSeqiNP_391536.1. NC_000964.3.
WP_003227751.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15672; CAB15672; BSU36550.
GeneIDi936951.
KEGGibsu:BSU36550.
PATRICi18979334. VBIBacSub10457_3829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69855.1.
AL009126 Genomic DNA. Translation: CAB15672.1.
PIRiB69713.
RefSeqiNP_391536.1. NC_000964.3.
WP_003227751.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TUFX-ray2.26B43-283[»]
3UZ0X-ray2.82B/D73-220[»]
ProteinModelPortaliP71044.
SMRiP71044. Positions 117-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60029N.
IntActiP71044. 1 interaction.
STRINGi224308.Bsubs1_010100019756.

Protein family/group databases

TCDBi1.A.34.1.1. 1.a.34 the bacillus gap junction-like channel-forming complex (gj-cc) family.

Proteomic databases

PaxDbiP71044.

Protocols and materials databases

DNASUi936951.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15672; CAB15672; BSU36550.
GeneIDi936951.
KEGGibsu:BSU36550.
PATRICi18979334. VBIBacSub10457_3829.

Phylogenomic databases

eggNOGiENOG4105FRN. Bacteria.
COG0739. LUCA.
HOGENOMiHOG000099586.
InParanoidiP71044.
KOiK06386.
OMAiTAVLWYQ.
OrthoDBiEOG64JFMH.

Enzyme and pathway databases

BioCyciBSUB:BSU36550-MONOMER.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Bacillus subtilis ureABC operon."
    Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.
    J. Bacteriol. 179:3371-3373(1997) [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. "SpoIIQ, a forespore-expressed gene required for engulfment in Bacillus subtilis."
    Londono-Vallejo J.A., Frehel C., Stragier P.
    Mol. Microbiol. 24:29-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  4. "A dispensable role for forespore-specific gene expression in engulfment of the forespore during sporulation of Bacillus subtilis."
    Sun Y.-L., Sharp M.D., Pogliano K.
    J. Bacteriol. 182:2919-2927(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis."
    Rubio A., Pogliano K.
    EMBO J. 23:1636-1646(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization."
    Blaylock B., Jiang X., Rubio A., Moran C.P. Jr., Pogliano K.
    Genes Dev. 18:2916-2928(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SPOIIIAH.
  7. "Developmental commitment in a bacterium."
    Dworkin J., Losick R.
    Cell 121:401-409(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum."
    Doan T., Marquis K.A., Rudner D.Z.
    Mol. Microbiol. 55:1767-1781(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SPOIIIAH.
  9. "Engulfment-regulated proteolysis of SpoIIQ: evidence that dual checkpoints control sigma activity."
    Jiang X., Rubio A., Chiba S., Pogliano K.
    Mol. Microbiol. 58:102-115(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEGRADATION.
  10. "Forespore engulfment mediated by a ratchet-like mechanism."
    Broder D.H., Pogliano K.
    Cell 126:917-928(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Dual localization pathways for the engulfment proteins during Bacillus subtilis sporulation."
    Aung S., Shum J., Abanes-De Mello A., Broder D.H., Fredlund-Gutierrez J., Chiba S., Pogliano K.
    Mol. Microbiol. 65:1534-1546(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "SpoIIQ anchors membrane proteins on both sides of the sporulation septum in Bacillus subtilis."
    Campo N., Marquis K.A., Rudner D.Z.
    J. Biol. Chem. 283:4975-4982(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPOIIE AND SPOIIIAH.
  13. "A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels."
    Camp A.H., Losick R.
    Mol. Microbiol. 69:402-417(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A channel connecting the mother cell and forespore during bacterial endospore formation."
    Meisner J., Wang X., Serrano M., Henriques A.O., Moran C.P. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 105:15100-15105(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPOIIIAH.

Entry informationi

Entry nameiSP2Q_BACSU
AccessioniPrimary (citable) accession number: P71044
Secondary accession number(s): Q795A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 1, 1997
Last modified: February 17, 2016
This is version 91 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

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.