ID   CYSC1_BACSU             Reviewed;         197 AA.
AC   O34577;
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=Probable adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=APS kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
GN   Name=cysC; Synonyms=ylnC; OrderedLocusNames=BSU15600;
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   -!- FUNCTION: Catalyzes the synthesis of activated sulfate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:456216; EC=2.7.1.25;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3.
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 APS kinase 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; AJ000974; CAA04412.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13434.1; -; Genomic_DNA.
DR   PIR; C69877; C69877.
DR   RefSeq; NP_389443.1; NC_000964.3.
DR   RefSeq; WP_003232097.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34577; -.
DR   SMR; O34577; -.
DR   IntAct; O34577; 1.
DR   MINT; O34577; -.
DR   STRING; 224308.BSU15600; -.
DR   PaxDb; O34577; -.
DR   PRIDE; O34577; -.
DR   EnsemblBacteria; CAB13434; CAB13434; BSU_15600.
DR   GeneID; 937102; -.
DR   KEGG; bsu:BSU15600; -.
DR   PATRIC; fig|224308.179.peg.1700; -.
DR   eggNOG; COG0529; Bacteria.
DR   InParanoid; O34577; -.
DR   OMA; DIVWHEA; -.
DR   PhylomeDB; O34577; -.
DR   BioCyc; BSUB:BSU15600-MON; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR   CDD; cd02027; APSK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..197
FT                   /note="Probable adenylyl-sulfate kinase"
FT                   /id="PRO_0000105903"
FT   ACT_SITE        107
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   197 AA;  22544 MW;  E5B69D3CDC0E5ECD CRC64;
     MTNRDIVWHE ASITKEEYQQ KNKHKSSILW LTGLSGSGKS TIANAAAREL FEQGYQVIVL
     DGDNIRHGLN RDLGFSDEDR KENIRRIGEV AKLFVQQGTI VITAFISPFR EDRQQVRELV
     EAGEFNEVYI KCDLDICEQR DPKGLYKKAR NGEIPFFTGI DSPYEEPEAP ELVLDSGQHD
     REACKNQLIE FVKQKLS