SAPB_BACSU
ID SAPB_BACSU Reviewed; 232 AA.
AC Q45514;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein SapB;
GN Name=sapB; OrderedLocusNames=BSU06650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP ALA-111, AND DEVELOPMENTAL STAGE.
RC STRAIN=168;
RX PubMed=9043134; DOI=10.1099/00221287-143-2-577;
RA Whalen M.B., Piggot P.J.;
RT "Gain-of-function mutation of sapB that affects formation of alkaline
RT phosphatase by Bacillus subtilis in sporulation conditions.";
RL Microbiology 143:577-583(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=168 / JH642;
RX PubMed=11902719; DOI=10.1046/j.1365-2958.1997.4441809.x;
RA von Blohn C., Kempf B., Kappes R.M., Bremer E.;
RT "Osmostress response in Bacillus subtilis: characterization of a proline
RT uptake system (OpuE) regulated by high osmolarity and the alternative
RT transcription factor sigma B.";
RL Mol. Microbiol. 25:175-187(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-232.
RC STRAIN=168;
RX PubMed=9701819; DOI=10.1046/j.1365-2958.1998.00927.x;
RA Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D.,
RA Bruand C.;
RT "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling
RT functions both in repair and rolling-circle replication.";
RL Mol. Microbiol. 29:261-273(1998).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Induced during late exponential phase, and maximum
CC expression is reached during the first hour of stationary phase, both
CC under sporulation and non-sporulation conditions.
CC {ECO:0000269|PubMed:9043134}.
CC -!- DISRUPTION PHENOTYPE: Cells activate alkaline phosphatase during
CC sporulation; the same phenotype is seen in the sapB2 and sapB10
CC mutants. {ECO:0000269|PubMed:9043134}.
CC -!- SIMILARITY: Belongs to the MgtC/SapB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U59128; AAB03321.1; -; Genomic_DNA.
DR EMBL; AF011545; AAB72181.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12485.1; -; Genomic_DNA.
DR EMBL; U92466; AAB66515.1; -; Genomic_DNA.
DR EMBL; Y15254; CAA75555.1; -; Genomic_DNA.
DR PIR; G69703; G69703.
DR RefSeq; NP_388547.1; NC_000964.3.
DR RefSeq; WP_010886431.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; Q45514; -.
DR SMR; Q45514; -.
DR STRING; 224308.BSU06650; -.
DR PaxDb; Q45514; -.
DR PRIDE; Q45514; -.
DR EnsemblBacteria; CAB12485; CAB12485; BSU_06650.
DR GeneID; 936054; -.
DR KEGG; bsu:BSU06650; -.
DR PATRIC; fig|224308.43.peg.702; -.
DR eggNOG; COG1285; Bacteria.
DR InParanoid; Q45514; -.
DR OMA; NHITMDP; -.
DR PhylomeDB; Q45514; -.
DR BioCyc; BSUB:BSU06650-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 InterPro; IPR003416; MgtC/SapB/SrpB/YhiD_fam.
DR PANTHER; PTHR33778; PTHR33778; 1.
DR Pfam; PF02308; MgtC; 1.
DR PRINTS; PR01837; MGTCSAPBPROT.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..232
FT /note="Protein SapB"
FT /id="PRO_0000202030"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 111
FT /note="A->T: In sapB2 and sapB10; activates alkaline
FT phosphatase during sporulation."
FT /evidence="ECO:0000269|PubMed:9043134"
SQ SEQUENCE 232 AA; 25936 MW; E0DBC13CCB161BA5 CRC64;
MLLSWYIDPD ILLKLGIATL IGMVIGLERE LKNKPLGLKT CIVIAVSSCM LTIVSINAAY
HFPKYYRIMM DPLRLPAQII SGVGFIGAGV ILRKSNDVIS GLTTSAMIWG AAGLGLATGA
GFYKEAFASL LFILISVEFL PWVVRKIGPD RLQEKDIRIR MSLSDKDKMT EILKEMKRRD
IKAHSVRIDD LGEKDFPIME VKVRVHKNRY TTDVYYDIKA IEGVVGVKCD TL
