(data stored in SCRATCH zone)

SWISSPROT: SP3AH_BACSU

ID   SP3AH_BACSU             Reviewed;         218 AA.
AC   P49785;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=Stage III sporulation protein AH;
GN   Name=spoIIIAH; OrderedLocusNames=BSU24360;
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 / JH642;
RA   Guerout-Fleury A.M., Gonzy-Treboul G., Stragier P.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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   [4]
RP   SEQUENCE REVISION TO 155.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIIQ.
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   [6]
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   SPOIIQ.
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   [7]
RP   FUNCTION.
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   [8]
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   [9]
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   [10]
RP   INTERACTION WITH SPOIIQ.
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   [11]
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   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIIQ.
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. Forms a channel with
CC       SpoIIIAH that is open on the forespore end and closed (or gated) on the
CC       mother cell end. This allows sigma-E-directed gene expression in the
CC       mother-cell compartment of the sporangium to trigger the activation of
CC       sigma-G forespore-specific gene expression by a pathway of
CC       intercellular signaling. {ECO:0000269|PubMed:15574594,
CC       ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:16164552,
CC       ECO:0000269|PubMed:16959571, ECO:0000269|PubMed:17824930,
CC       ECO:0000269|PubMed:18485064, ECO:0000269|PubMed:18812514}.
CC   -!- SUBUNIT: Interacts with SpoIIQ. {ECO:0000269|PubMed:15574594,
CC       ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18077456,
CC       ECO:0000269|PubMed:18812514}.
CC   -!- INTERACTION:
CC       P71044:spoIIQ; NbExp=13; IntAct=EBI-6413215, EBI-6413220;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Note=Localizes to the engulfing septal membranes
CC       during spore formation. {ECO:0000269|PubMed:15574594,
CC       ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18812514}.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in the mother cell during
CC       sporulation under the control of the sigma-E factor.
CC       {ECO:0000269|PubMed:15752199}.
DR   EMBL; U35252; AAA76727.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12567.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14367.2; -; Genomic_DNA.
DR   PIR; C69712; C69712.
DR   RefSeq; NP_390316.2; NC_000964.3.
DR   RefSeq; WP_003230250.1; NZ_JNCM01000036.1.
DR   PDB; 3TUF; X-ray; 2.26 A; A=25-218.
DR   PDB; 3UZ0; X-ray; 2.82 A; A/C=90-218.
DR   PDBsum; 3TUF; -.
DR   PDBsum; 3UZ0; -.
DR   SMR; P49785; -.
DR   DIP; DIP-60030N; -.
DR   IntAct; P49785; 1.
DR   STRING; 224308.BSU24360; -.
DR   TCDB; 1.A.34.1.1; the bacillus gap junction-like channel-forming complex (gj-cc) family.
DR   PaxDb; P49785; -.
DR   PRIDE; P49785; -.
DR   EnsemblBacteria; CAB14367; CAB14367; BSU24360.
DR   GeneID; 938600; -.
DR   KEGG; bsu:BSU24360; -.
DR   PATRIC; fig|224308.179.peg.2654; -.
DR   HOGENOM; HOG000096672; -.
DR   KO; K06397; -.
DR   OMA; KSEAYDK; -.
DR   BioCyc; BSUB:BSU24360-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   DisProt; DP00862; -.
DR   Gene3D; 3.30.300.270; -; 1.
DR   InterPro; IPR024232; SpoIIIAH.
DR   InterPro; IPR038503; SpoIIIAH_sf.
DR   Pfam; PF12685; SpoIIIAH; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P49785.
DR   SWISS-2DPAGE; P49785.
KW   3D-structure; Cell membrane; Membrane; Reference proteome; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..218
FT                   /note="Stage III sporulation protein AH"
FT                   /id="PRO_0000072072"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        155
FT                   /note="E -> G (in Ref. 2; BAA12567)"
FT                   /evidence="ECO:0000305"
FT   HELIX           105..128
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   STRAND          131..133
FT                   /evidence="ECO:0000244|PDB:3UZ0"
FT   HELIX           135..164
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   STRAND          170..173
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   STRAND          175..184
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   HELIX           190..198
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   HELIX           202..205
FT                   /evidence="ECO:0000244|PDB:3TUF"
FT   STRAND          208..215
FT                   /evidence="ECO:0000244|PDB:3TUF"
SQ   SEQUENCE   218 AA;  23806 MW;  CD0F17364320445A CRC64;
     MLKKQTVWLL TMLSLVVVLS VYYIMSPESK NAVQMQSEKS ASDSGEVATE KAPAKQDTKE
     KSGTETEKGK EDGTKGTKDS SADKETSAEA SEKGTVVTET ADDDLFTTYR LDLEDARSKE
     REELNAIVSS DDATAKEKSE AYDKMTALSE VEGTEKQLET LIKTQGYEDA LVNAEGDKIN
     ITVKSDKHSK SKATAIIDLV AKEIKTMKDV AVTFEPSK
//

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