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 03-AUG-2022, entry version 114.
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 P49785; 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}.
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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 AlphaFoldDB; P49785; -.
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; BSU_24360.
DR GeneID; 938600; -.
DR KEGG; bsu:BSU24360; -.
DR PATRIC; fig|224308.179.peg.2654; -.
DR eggNOG; ENOG5030IKQ; Bacteria.
DR OMA; VYYIMSP; -.
DR BioCyc; BSUB:BSU24360-MON; -.
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; 1.10.287.4300; -; 1.
DR InterPro; IPR024232; SpoIIIAH.
DR InterPro; IPR038503; SpoIIIAH_sf.
DR Pfam; PF12685; SpoIIIAH; 1.
PE 1: Evidence at protein level;
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 REGION 33..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 155
FT /note="E -> G (in Ref. 2; BAA12567)"
FT /evidence="ECO:0000305"
FT HELIX 105..128
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3UZ0"
FT HELIX 135..164
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:3TUF"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3TUF"
FT STRAND 208..215
FT /evidence="ECO:0007829|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
