ID   SAT1_BACSU              Reviewed;         382 AA.
AC   O34764;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Sulfate adenylyltransferase;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=sat; Synonyms=ylnB; OrderedLocusNames=BSU15590;
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   Foulger D., Errington J.;
RT   "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of
RT   the pyr operon.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   INDUCTION.
RC   STRAIN=168 / JH642;
RX   PubMed=11004190; DOI=10.1128/jb.182.20.5885-5892.2000;
RA   Mansilla M.C., Albanesi D., de Mendoza D.;
RT   "Transcriptional control of the sulfur-regulated cysH operon, containing
RT   genes involved in L-cysteine biosynthesis in Bacillus subtilis.";
RL   J. Bacteriol. 182:5885-5892(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3.
CC   -!- INDUCTION: Up-regulated by sulfur starvation and repressed by cysteine.
CC       Also induced by O-acetyl-L-serine (OAS), a direct precursor of
CC       cysteine, maybe via inactivation of a putative transcriptional
CC       repressor of the cysH operon whose activity is controlled by the
CC       intracellular levels of OAS. {ECO:0000269|PubMed:11004190}.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ000974; CAA04411.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13433.1; -; Genomic_DNA.
DR   PIR; B69877; B69877.
DR   RefSeq; NP_389442.1; NC_000964.3.
DR   RefSeq; WP_003245745.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34764; -.
DR   SMR; O34764; -.
DR   IntAct; O34764; 2.
DR   MINT; O34764; -.
DR   STRING; 224308.BSU15590; -.
DR   PaxDb; O34764; -.
DR   PRIDE; O34764; -.
DR   EnsemblBacteria; CAB13433; CAB13433; BSU_15590.
DR   GeneID; 936726; -.
DR   KEGG; bsu:BSU15590; -.
DR   PATRIC; fig|224308.179.peg.1699; -.
DR   eggNOG; COG2046; Bacteria.
DR   InParanoid; O34764; -.
DR   OMA; LQHMIIR; -.
DR   PhylomeDB; O34764; -.
DR   BioCyc; BSUB:BSU15590-MON; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd00517; ATPS; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00339; sopT; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..382
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_0000105937"
SQ   SEQUENCE   382 AA;  42884 MW;  1E9856F3A9AD21E3 CRC64;
     MSLAPHGGTL VNRVDESYDV SGIQKEIELD LISFADLELI GIGAYSPIEG FFNEKDYVSV
     VENMRLSSGV VWSLPITLPV DAQKAAELSL GETVKLTYEG ETYGVIQIED LYVPDKQKEA
     VNVYKTDEQE HPGVKKLFSR GNTYVGGPIT LIKKASKQFP EFTFEPSETR RQFAEKGWET
     IVGFQTRNPV HRAHEYIQKT ALETVDGLFL NPLVGETKSD DIPADVRMES YQVLLDHYYP
     KDRVFLGVFL AAMRYAGPRE AIFHALVRKN YGCTHFIVGR DHAGVGDYYG TYEAQELFDT
     FKPEELGITP LKFEHSFFCK KCGNMGTAKT CPHGREHHVI LSGTKVRGML RDGVLPPAEF
     SRKEVVEVLI KGMKKKEEVG VS