SP2Q_BACSU
ID SP2Q_BACSU Reviewed; 283 AA.
AC P71044; Q795A1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Stage II sporulation protein Q;
GN Name=spoIIQ; Synonyms=ywnI; OrderedLocusNames=BSU36550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9150240; DOI=10.1128/jb.179.10.3371-3373.1997;
RA Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.;
RT "The Bacillus subtilis ureABC operon.";
RL J. Bacteriol. 179:3371-3373(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=9140963; DOI=10.1046/j.1365-2958.1997.3181680.x;
RA Londono-Vallejo J.A., Frehel C., Stragier P.;
RT "SpoIIQ, a forespore-expressed gene required for engulfment in Bacillus
RT subtilis.";
RL Mol. Microbiol. 24:29-39(1997).
RN [4]
RP FUNCTION.
RX PubMed=10781563; DOI=10.1128/jb.182.10.2919-2927.2000;
RA Sun Y.-L., Sharp M.D., Pogliano K.;
RT "A dispensable role for forespore-specific gene expression in engulfment of
RT the forespore during sporulation of Bacillus subtilis.";
RL J. Bacteriol. 182:2919-2927(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15044948; DOI=10.1038/sj.emboj.7600171;
RA Rubio A., Pogliano K.;
RT "Septal localization of forespore membrane proteins during engulfment in
RT Bacillus subtilis.";
RL EMBO J. 23:1636-1646(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIIIAH.
RX PubMed=15574594; DOI=10.1101/gad.1252704;
RA Blaylock B., Jiang X., Rubio A., Moran C.P. Jr., Pogliano K.;
RT "Zipper-like interaction between proteins in adjacent daughter cells
RT mediates protein localization.";
RL Genes Dev. 18:2916-2928(2004).
RN [7]
RP FUNCTION.
RX PubMed=15882622; DOI=10.1016/j.cell.2005.02.032;
RA Dworkin J., Losick R.;
RT "Developmental commitment in a bacterium.";
RL Cell 121:401-409(2005).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SPOIIIAH.
RX PubMed=15752199; DOI=10.1111/j.1365-2958.2005.04501.x;
RA Doan T., Marquis K.A., Rudner D.Z.;
RT "Subcellular localization of a sporulation membrane protein is achieved
RT through a network of interactions along and across the septum.";
RL Mol. Microbiol. 55:1767-1781(2005).
RN [9]
RP FUNCTION, AND DEGRADATION.
RX PubMed=16164552; DOI=10.1111/j.1365-2958.2005.04811.x;
RA Jiang X., Rubio A., Chiba S., Pogliano K.;
RT "Engulfment-regulated proteolysis of SpoIIQ: evidence that dual checkpoints
RT control sigma activity.";
RL Mol. Microbiol. 58:102-115(2005).
RN [10]
RP FUNCTION.
RX PubMed=16959571; DOI=10.1016/j.cell.2006.06.053;
RA Broder D.H., Pogliano K.;
RT "Forespore engulfment mediated by a ratchet-like mechanism.";
RL Cell 126:917-928(2006).
RN [11]
RP FUNCTION.
RX PubMed=17824930; DOI=10.1111/j.1365-2958.2007.05887.x;
RA Aung S., Shum J., Abanes-De Mello A., Broder D.H., Fredlund-Gutierrez J.,
RA Chiba S., Pogliano K.;
RT "Dual localization pathways for the engulfment proteins during Bacillus
RT subtilis sporulation.";
RL Mol. Microbiol. 65:1534-1546(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIIE AND SPOIIIAH.
RX PubMed=18077456; DOI=10.1074/jbc.m708024200;
RA Campo N., Marquis K.A., Rudner D.Z.;
RT "SpoIIQ anchors membrane proteins on both sides of the sporulation septum
RT in Bacillus subtilis.";
RL J. Biol. Chem. 283:4975-4982(2008).
RN [13]
RP FUNCTION.
RX PubMed=18485064; DOI=10.1111/j.1365-2958.2008.06289.x;
RA Camp A.H., Losick R.;
RT "A novel pathway of intercellular signalling in Bacillus subtilis involves
RT a protein with similarity to a component of type III secretion channels.";
RL Mol. Microbiol. 69:402-417(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIIIAH.
RX PubMed=18812514; DOI=10.1073/pnas.0806301105;
RA Meisner J., Wang X., Serrano M., Henriques A.O., Moran C.P. Jr.;
RT "A channel connecting the mother cell and forespore during bacterial
RT endospore formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15100-15105(2008).
CC -!- FUNCTION: Involved in forespore engulfment and required for anchoring
CC membrane proteins on the forespore side of the septal membrane. Forms a
CC channel with SpoIIIAH that is open on the forespore end and closed (or
CC gated) on the mother cell end. This allows sigma-E-directed gene
CC expression in the mother-cell compartment of the sporangium to trigger
CC the activation of sigma-G forespore-specific gene expression by a
CC pathway of intercellular signaling. {ECO:0000269|PubMed:10781563,
CC ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:15882622,
CC ECO:0000269|PubMed:16164552, ECO:0000269|PubMed:16959571,
CC ECO:0000269|PubMed:17824930, ECO:0000269|PubMed:18077456,
CC ECO:0000269|PubMed:18485064, ECO:0000269|PubMed:18812514,
CC ECO:0000269|PubMed:9140963}.
CC -!- SUBUNIT: Interacts with SpoIIIAH and SpoIIE.
CC {ECO:0000269|PubMed:15574594, ECO:0000269|PubMed:15752199,
CC ECO:0000269|PubMed:18077456, ECO:0000269|PubMed:18812514}.
CC -!- INTERACTION:
CC P71044; P49785: spoIIIAH; NbExp=13; IntAct=EBI-6413220, EBI-6413215;
CC -!- SUBCELLULAR LOCATION: Forespore membrane {ECO:0000269|PubMed:15044948,
CC ECO:0000269|PubMed:15574594, ECO:0000269|PubMed:15752199,
CC ECO:0000269|PubMed:18077456, ECO:0000269|PubMed:18812514,
CC ECO:0000269|PubMed:9140963}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15044948, ECO:0000269|PubMed:15574594,
CC ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18077456,
CC ECO:0000269|PubMed:18812514, ECO:0000269|PubMed:9140963}.
CC Note=Localizes to the engulfing septal membranes.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the forespore under the
CC control of the sigma-K factor. {ECO:0000269|PubMed:15752199,
CC ECO:0000269|PubMed:9140963}.
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DR EMBL; Y08559; CAA69855.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15672.1; -; Genomic_DNA.
DR PIR; B69713; B69713.
DR RefSeq; NP_391536.1; NC_000964.3.
DR RefSeq; WP_003227751.1; NZ_JNCM01000034.1.
DR PDB; 3TUF; X-ray; 2.26 A; B=43-283.
DR PDB; 3UZ0; X-ray; 2.82 A; B/D=73-220.
DR PDBsum; 3TUF; -.
DR PDBsum; 3UZ0; -.
DR AlphaFoldDB; P71044; -.
DR SMR; P71044; -.
DR DIP; DIP-60029N; -.
DR IntAct; P71044; 1.
DR STRING; 224308.BSU36550; -.
DR TCDB; 1.A.34.1.1; the bacillus gap junction-like channel-forming complex (gj-cc) family.
DR TCDB; 9.B.70.1.1; the multicomponent putative spoiiiae exporter (spoiiia-e) family.
DR PaxDb; P71044; -.
DR DNASU; 936951; -.
DR EnsemblBacteria; CAB15672; CAB15672; BSU_36550.
DR GeneID; 936951; -.
DR KEGG; bsu:BSU36550; -.
DR PATRIC; fig|224308.179.peg.3955; -.
DR eggNOG; COG0739; Bacteria.
DR InParanoid; P71044; -.
DR OMA; FFRKRWV; -.
DR BioCyc; BSUB:BSU36550-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042601; C:endospore-forming forespore; IMP:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Stage II sporulation protein Q"
FT /id="PRO_0000360550"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 228..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3UZ0"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3TUF"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3UZ0"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3TUF"
SQ SEQUENCE 283 AA; 31113 MW; E913200AF563C98C CRC64;
MREEEKKTSQ VKKLQQFFRK RWVFPAIYLV SAAVILTAVL WYQSVSNDEV KDQLADNGGN
SAYDNNDDAV EVGKSMENVA MPVVDSENVS VVKKFYETDA AKEEKEAALV TYNNTYSLSK
GIDLAEKDGK DFDVSASLSG TVVKAEKDPV LGYVVEVEHA DGLSTVYQSL SEVSVEQGDK
VKQNQVIGKS GKNLYSEDSG NHVHFEIRKD GVAMNPLNFM DKPVSSIEKA ATQETEESIQ
QSSEKKDGST EKGTEEKSGE KKDDSTDKSG SKESSTTEDT EQS
