SAFA_BACSU
ID SAFA_BACSU Reviewed; 387 AA.
AC O32062; O52861; Q799D6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=SpoIVD-associated factor A;
DE AltName: Full=Morphogenetic protein SafA;
GN Name=safA; Synonyms=yrbA; OrderedLocusNames=BSU27840;
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;
RA Tosato V., Bolotin A., Bertani I., Valentino I., Bruschi C.V.;
RT "A 17.8 kb segment in the spoVB-nadC region of the Bacillus subtilis 168
RT chromosome: sequencing and ruv operon identification.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / 60015;
RX PubMed=9770294; DOI=10.1111/j.1574-6968.1998.tb13913.x;
RA Takamatsu H., Hiraoka T., Kodama T., Koide H., Kozuka S., Tochikubo K.,
RA Watabe K.;
RT "Cloning of a novel gene yrbB, encoding a protein located in the spore
RT integument of Bacillus subtilis.";
RL FEMS Microbiol. Lett. 166:361-367(1998).
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 PROTEIN SEQUENCE OF 164-172, TRANSCRIPTION, AND MUTANT STUDIES.
RC STRAIN=168;
RX PubMed=10438771; DOI=10.1128/jb.181.16.4986-4994.1999;
RA Takamatsu H., Kodama T., Nakayama T., Watabe K.;
RT "Characterization of the yrbA gene of Bacillus subtilis, involved in
RT resistance and germination of spores.";
RL J. Bacteriol. 181:4986-4994(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH SPOIVD.
RC STRAIN=168;
RX PubMed=10714986; DOI=10.1128/jb.182.7.1828-1833.2000;
RA Ozin A.J., Henriques A.O., Yi H., Moran C.P. Jr.;
RT "Morphogenetic proteins SpoVID and SafA form a complex during assembly of
RT the Bacillus subtilis spore coat.";
RL J. Bacteriol. 182:1828-1833(2000).
CC -!- FUNCTION: Probably involved in the assembly of some coat protein
CC components implicated in both lysozyme resistance and germination.
CC Could be required for the assembly of CotG. Associates with SpoIVD
CC during the early stage of coat assembly.
CC -!- SUBCELLULAR LOCATION: Spore cortex {ECO:0000269|PubMed:10714986}.
CC Note=At the coat-cortex interface.
CC -!- INDUCTION: Transcribed by SigE at time T2 of sporulation.
CC -!- MISCELLANEOUS: Several coat proteins are extracted in reduced amounts
CC from SafA mutant spores, one of which is CotG. SafA mutant spores have
CC abnormal coat layers and have lost their resistance to lysozyme. Their
CC response to L-alanine suggest that they have a defect at a late stage
CC of spore germination. Their response to AGFK also suggests that they
CC have an additional defect at a early stage of spore germination. The
CC mutation of SafA has no effect on vegetative growth and spore
CC resistance to heat and chloroform.
CC -!- MISCELLANEOUS: In wild-type cells, during the early stages of
CC sporulation, a product of 43 kDa (the predicted size of SafA) was
CC detected. However, in later stages, a 30-kDa species was the major form
CC of SafA detected. The N-terminus sequence of the 30-kDa product starts
CC at Met-164. It is not known if the smaller form results from
CC proteolysis or from translation initiated at Met-164.
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DR EMBL; Y15896; CAB75322.1; -; Genomic_DNA.
DR EMBL; D50551; BAA24943.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14744.1; -; Genomic_DNA.
DR PIR; H69971; H69971.
DR RefSeq; NP_390662.1; NC_000964.3.
DR RefSeq; WP_003229695.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O32062; -.
DR SMR; O32062; -.
DR IntAct; O32062; 1.
DR STRING; 224308.BSU27840; -.
DR PaxDb; O32062; -.
DR PRIDE; O32062; -.
DR EnsemblBacteria; CAB14744; CAB14744; BSU_27840.
DR GeneID; 937514; -.
DR KEGG; bsu:BSU27840; -.
DR PATRIC; fig|224308.179.peg.3025; -.
DR eggNOG; COG1388; Bacteria.
DR OMA; EFKPEFK; -.
DR BioCyc; BSUB:BSU27840-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043595; C:endospore cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR014248; Spore_coat_assembly_SafA.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR TIGRFAMs; TIGR02899; spore_safA; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Sporulation.
FT CHAIN 1..387
FT /note="SpoIVD-associated factor A"
FT /id="PRO_0000246074"
FT DOMAIN 2..47
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 49..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 184
FT /note="I -> V (in Ref. 2; BAA24943)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Y -> F (in Ref. 2; BAA24943)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> T (in Ref. 2; BAA24943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43229 MW; CE619293E809E5D4 CRC64;
MKIHIVQKGD SLWKIAEKYG VDVEEVKKLN TQLSNPDLIM PGMKIKVPSE GVPVRKEPKA
GKSPAAGSVK QEHPYAKEKP KSVVDVEDTK PKEKKSMPYV PPMPNLQENV YPEADVNDYY
DMKQLFQPWS PPKPEEPKKH HDGNMDHMYH MQDQFPQQEA MSNMENANYP NMPNMPKAPE
VGGIEEENVH HTVPNMPMPA VQPYYHYPAH FVPCPVPVSP ILPGSGLCYP YYPAQAYPMH
PMHGYQPGFV SPQYDPGYEN QHHENSHHGH YGSYGAPQYA SPAYGSPYGH MPYGPYYGTP
QVMGAYQPAA AHGYMPYKDH DDCGCDGDHQ PYFSAPGHSG MGAYGSPNMP YGTANPNPNP
YSAGVSMPMT NQPSVNQMFG RPEEENE
