ID   ABRB_BACSU              Reviewed;          96 AA.
AC   P08874;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Transition state regulatory protein AbrB;
GN   Name=abrB; Synonyms=cpsX; OrderedLocusNames=BSU00370;
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=3145384; DOI=10.1111/j.1365-2958.1988.tb00079.x;
RA   Perego M., Spiegelman G.B., Hoch J.A.;
RT   "Structure of the gene for the transition state regulator, abrB: regulator
RT   synthesis is controlled by the spo0A sporulation gene in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 2:689-699(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2554317; DOI=10.1073/pnas.86.21.8457;
RA   Robertson J.R., Gocht M., Marahiel M.A., Zuber P.;
RT   "AbrB, a regulator of gene expression in Bacillus, interacts with the
RT   transcription initiation regions of a sporulation gene and an antibiotic
RT   biosynthesis gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8457-8461(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [4]
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   [5]
RP   FUNCTION.
RX   PubMed=2504584; DOI=10.1002/j.1460-2075.1989.tb03546.x;
RA   Strauch M.A., Spiegelman G.B., Perego M., Johnson W.C., Burbulys D.,
RA   Hoch J.A.;
RT   "The transition state transcription regulator abrB of Bacillus subtilis is
RT   a DNA binding protein.";
RL   EMBO J. 8:1615-1621(1989).
RN   [6]
RP   CHARACTERIZATION, AND MUTAGENESIS OF CYS-56.
RX   PubMed=1908787; DOI=10.1016/0014-5793(91)80038-5;
RA   Fuerbass R., Marahiel M.A.;
RT   "Mutant analysis of interaction of the Bacillus subtilis transcription
RT   regulator AbrB with the antibiotic biosynthesis gene tycA.";
RL   FEBS Lett. 287:153-156(1991).
RN   [7]
RP   ABRB-REGULATED GENES.
RX   PubMed=15101989; DOI=10.1111/j.1365-2958.2004.04023.x;
RA   Hamon M.A., Stanley N.R., Britton R.A., Grossman A.D., Lazazzera B.A.;
RT   "Identification of AbrB-regulated genes involved in biofilm formation by
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 52:847-860(2004).
RN   [8]
RP   INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX   PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA   Gaballa A., Su T.T., Helmann J.D.;
RT   "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT   (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL   Redox Biol. 42:101935-101935(2021).
CC   -!- FUNCTION: Ambiactive repressor and activator of the transcription of
CC       genes expressed during the transition state between vegetative growth
CC       and the onset of stationary phase and sporulation. It controls the
CC       expression of genes spovG and tycA. AbrB binds to the tycA promoter
CC       region at two A- and T-rich sites, it may be the sole repressor of tycA
CC       transcription. {ECO:0000269|PubMed:2504584}.
CC   -!- SUBUNIT: Interacts with BrxC. {ECO:0000269|PubMed:33722570}.
CC   -!- INTERACTION:
CC       P08874; P08874: abrB; NbExp=4; IntAct=EBI-2121787, EBI-2121787;
CC       P08874; O31697: ykzF; NbExp=2; IntAct=EBI-2121787, EBI-15732529;
CC   -!- SIMILARITY: To B.subtilis Abh and SpoVT. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22195.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA43955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; X12820; CAA31307.1; -; Genomic_DNA.
DR   EMBL; M26917; AAA22195.1; ALT_INIT; Genomic_DNA.
DR   EMBL; D26185; BAA05272.1; -; Genomic_DNA.
DR   EMBL; X61953; CAA43955.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB11813.1; -; Genomic_DNA.
DR   PIR; S03096; S03096.
DR   RefSeq; NP_387918.1; NC_000964.3.
DR   RefSeq; WP_003226760.1; NZ_JNCM01000028.1.
DR   PDB; 1YFB; NMR; -; A/B=2-53.
DR   PDB; 1YSF; NMR; -; A/B=2-53.
DR   PDB; 1Z0R; NMR; -; A/B=3-55.
DR   PDB; 2K1N; NMR; -; A/B/C/D=3-57.
DR   PDB; 2MJG; NMR; -; A/B=54-96.
DR   PDB; 2RO4; NMR; -; A/B=3-55.
DR   PDBsum; 1YFB; -.
DR   PDBsum; 1YSF; -.
DR   PDBsum; 1Z0R; -.
DR   PDBsum; 2K1N; -.
DR   PDBsum; 2MJG; -.
DR   PDBsum; 2RO4; -.
DR   AlphaFoldDB; P08874; -.
DR   BMRB; P08874; -.
DR   SMR; P08874; -.
DR   DIP; DIP-46306N; -.
DR   IntAct; P08874; 1.
DR   STRING; 224308.BSU00370; -.
DR   jPOST; P08874; -.
DR   PaxDb; P08874; -.
DR   PRIDE; P08874; -.
DR   EnsemblBacteria; CAB11813; CAB11813; BSU_00370.
DR   GeneID; 50135239; -.
DR   GeneID; 937009; -.
DR   KEGG; bsu:BSU00370; -.
DR   PATRIC; fig|224308.43.peg.38; -.
DR   eggNOG; COG2002; Bacteria.
DR   OMA; DRHYAGN; -.
DR   PhylomeDB; P08874; -.
DR   BioCyc; BSUB:BSU00370-MON; -.
DR   EvolutionaryTrace; P08874; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CACAO.
DR   GO; GO:0043937; P:regulation of sporulation; IGI:CACAO.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR040678; AbrB_C.
DR   InterPro; IPR007159; SpoVT-AbrB_dom.
DR   InterPro; IPR037914; SpoVT-AbrB_sf.
DR   Pfam; PF18277; AbrB_C; 1.
DR   Pfam; PF04014; MazE_antitoxin; 1.
DR   SMART; SM00966; SpoVT_AbrB; 1.
DR   SUPFAM; SSF89447; SSF89447; 1.
DR   TIGRFAMs; TIGR01439; lp_hng_hel_AbrB; 1.
DR   PROSITE; PS51740; SPOVT_ABRB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW   Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..96
FT                   /note="Transition state regulatory protein AbrB"
FT                   /id="PRO_0000064431"
FT   DOMAIN          7..52
FT                   /note="SpoVT-AbrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT   MUTAGEN         56
FT                   /note="C->Y: Loss of DNA-binding activity."
FT                   /evidence="ECO:0000269|PubMed:1908787"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:1YFB"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:1Z0R"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:1YFB"
FT   HELIX           22..27
FT                   /evidence="ECO:0007829|PDB:1YFB"
FT   STRAND          35..41
FT                   /evidence="ECO:0007829|PDB:1YFB"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:1YFB"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:2K1N"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:2MJG"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:2MJG"
FT   HELIX           78..93
FT                   /evidence="ECO:0007829|PDB:2MJG"
SQ   SEQUENCE   96 AA;  10773 MW;  6A964557F5590CFE CRC64;
     MFMKSTGIVR KVDELGRVVI PIELRRTLGI AEKDALEIYV DDEKIILKKY KPNMTCQVTG
     EVSDDNLKLA GGKLVLSKEG AEQIISEIQN QLQNLK