SACY_BACSU
ID SACY_BACSU Reviewed; 280 AA.
AC P15401;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Levansucrase and sucrase synthesis operon antiterminator;
GN Name=sacY; Synonyms=sacS; OrderedLocusNames=BSU38420; ORFNames=ipa-13r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2116367; DOI=10.1016/0378-1119(90)90453-x;
RA Zukowski M.M., Miller L., Cosgwell P., Chen K., Aymerich S., Steinmetz M.;
RT "Nucleotide sequence of the sacS locus of Bacillus subtilis reveals the
RT presence of two regulatory genes.";
RL Gene 90:153-155(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1806041; DOI=10.3109/10425179109020780;
RA Glaser P., Kunst F., Debarbouille M., Vertes A., Danchin A., Dedonder R.;
RT "A gene encoding a tyrosine tRNA synthetase is located near sacS in
RT Bacillus subtilis.";
RL DNA Seq. 1:251-261(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
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=8535520; DOI=10.1099/13500872-141-11-2921;
RA Tortosa P., Le Coq D.;
RT "A ribonucleic antiterminator sequence (RAT) and a distant palindrome are
RT both involved in sucrose induction of the Bacillus subtilis sacXY
RT regulatory operon.";
RL Microbiology 141:2921-2927(1995).
RN [6]
RP PHOSPHORYLATION AT HIS-99; HIS-207 AND HIS-269 BY HPR.
RX PubMed=9202047; DOI=10.1074/jbc.272.27.17230;
RA Tortosa P., Aymerich S., Lindner C., Saier M.H. Jr., Reizer J., Le Coq D.;
RT "Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional
RT antiterminator negatively controlled by the phosphotransferase system.";
RL J. Biol. Chem. 272:17230-17237(1997).
RN [7]
RP CRYSTALLIZATION OF THE RNA-BINDING DOMAIN.
RX PubMed=9261875;
RX DOI=10.1002/(sici)1097-0134(199708)28:4<590::aid-prot13>3.0.co;2-b;
RA Manival X., Aymerich S., Strub M.-P., Dumas C., Kochoyan M.,
RA van Tilbeurgh H.;
RT "Crystallization of the RNA-binding domain of the transcriptional
RT antiterminator protein SacY from Bacillus subtilis.";
RL Proteins 28:590-594(1997).
RN [8]
RP PHOSPHORYLATION AT HIS-99 BY SACX.
RX PubMed=11580842; DOI=10.1046/j.1365-2958.2001.02608.x;
RA Tortosa P., Declerck N., Dutartre H., Lindner C., Deutscher J., Le Coq D.;
RT "Sites of positive and negative regulation in the Bacillus subtilis
RT antiterminators LicT and SacY.";
RL Mol. Microbiol. 41:1381-1393(2001).
RN [9]
RP STRUCTURE BY NMR OF 1-55.
RX PubMed=9305643; DOI=10.1093/emboj/16.16.5019;
RA Manival X., Yang Y., Strub M.-P., Kochoyan M., Steinmetz M., Aymerich S.;
RT "From genetic to structural characterization of a new class of RNA-binding
RT domain within the SacY/BglG family of antiterminator proteins.";
RL EMBO J. 16:5019-5029(1997).
CC -!- FUNCTION: In the presence of sucrose, SacY is activated and prevents
CC premature termination of transcription by binding to a RNA-
CC antiterminator (RAT) sequence (partially overlapping with the
CC terminator sequence) located upstream of the sacB gene. Formation of
CC the SacY-RAT complex prevents alternative formation of the terminator,
CC allowing transcription of the sacB gene. In the absence of sucrose,
CC inhibition of SacY activity by SacX leads to termination of
CC transcription. {ECO:0000269|PubMed:8535520}.
CC -!- PTM: Phosphorylated by HPr (PtsH). Also phosphorylated by SacX on His-
CC 99, leading to its inactivation. {ECO:0000269|PubMed:11580842,
CC ECO:0000269|PubMed:9202047}.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC {ECO:0000305}.
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DR EMBL; M29333; AAA75336.1; -; Genomic_DNA.
DR EMBL; X52480; CAA36720.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51569.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15868.1; -; Genomic_DNA.
DR PIR; JU0294; JU0294.
DR RefSeq; NP_391721.1; NC_000964.3.
DR RefSeq; WP_003244589.1; NZ_JNCM01000034.1.
DR PDB; 1AUU; NMR; -; A/B=1-55.
DR PDBsum; 1AUU; -.
DR AlphaFoldDB; P15401; -.
DR BMRB; P15401; -.
DR SMR; P15401; -.
DR STRING; 224308.BSU38420; -.
DR iPTMnet; P15401; -.
DR PaxDb; P15401; -.
DR PRIDE; P15401; -.
DR EnsemblBacteria; CAB15868; CAB15868; BSU_38420.
DR GeneID; 937335; -.
DR KEGG; bsu:BSU38420; -.
DR PATRIC; fig|224308.179.peg.4159; -.
DR eggNOG; COG3711; Bacteria.
DR OMA; HESAMSI; -.
DR PhylomeDB; P15401; -.
DR BioCyc; BSUB:BSU38420-MON; -.
DR EvolutionaryTrace; P15401; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.30.24.10; -; 1.
DR InterPro; IPR004341; CAT_RNA-bd_dom.
DR InterPro; IPR036650; CAT_RNA-bd_dom_sf.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR001550; Transcrpt_antitermin_CS.
DR Pfam; PF03123; CAT_RBD; 1.
DR Pfam; PF00874; PRD; 2.
DR SMART; SM01061; CAT_RBD; 1.
DR SUPFAM; SSF50151; SSF50151; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS00654; PRD_1; 1.
DR PROSITE; PS51372; PRD_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..280
FT /note="Levansucrase and sucrase synthesis operon
FT antiterminator"
FT /id="PRO_0000204249"
FT DOMAIN 64..169
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 170..280
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT REGION 1..55
FT /note="RNA-binding"
FT MOD_RES 99
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704,
FT ECO:0000269|PubMed:11580842, ECO:0000269|PubMed:9202047"
FT MOD_RES 207
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704,
FT ECO:0000269|PubMed:9202047"
FT MOD_RES 269
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704,
FT ECO:0000269|PubMed:9202047"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1AUU"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1AUU"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1AUU"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1AUU"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1AUU"
SQ SEQUENCE 280 AA; 32466 MW; A6A8D7C6AFD44291 CRC64;
MKIKRILNHN AIVVKDQNEE KILLGAGIAF NKKKNDIVDP SKIEKTFIRK DTPDYKQFEE
ILETLPEDHI QISEQIISHA EKELNIKINE RIHVAFSDHL SFAIERLSNG MVIKNPLLNE
IKVLYPKEFQ IGLWARALIK DKLGIHIPDD EIGNIAMHIH TARNNAGDMT QTLDITTMIR
DIIEIIEIQL SINIVEDTIS YERLVTHLRF AIQHIKAGES IYELDAEMID IIKEKFKDAF
LCALSIGTFV KKEYGFEFPE KELCYIAMHI QRFYQRSVAR
