(data stored in SCRATCH zone)

SWISSPROT: CYSK_BACSU

ID   CYSK_BACSU              Reviewed;         308 AA.
AC   P37887;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 143.
DE   RecName: Full=Cysteine synthase;
DE            Short=CSase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL;
DE   AltName: Full=Superoxide-inducible protein 11;
DE            Short=SOI11;
GN   Name=cysK; OrderedLocusNames=BSU00730;
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=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   [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   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=168 / JH642;
RX   PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA   Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT   "Cold shock stress-induced proteins in Bacillus subtilis.";
RL   J. Bacteriol. 178:4611-4619(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [5]
RP   DETERMINATION OF TRANSCRIPTIONAL START SITE, DISRUPTION PHENOTYPE, AND
RP   INDUCTION.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=11445163; DOI=10.1111/j.1574-6968.2001.tb10728.x;
RA   van der Ploeg J.R., Barone M., Leisinger T.;
RT   "Functional analysis of the Bacillus subtilis cysK and cysJI genes.";
RL   FEMS Microbiol. Lett. 201:29-35(2001).
RN   [6]
RP   CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=17056751; DOI=10.1128/jb.01273-06;
RA   Hullo M.-F., Auger S., Soutourina O., Barzu O., Yvon M., Danchin A.,
RA   Martin-Verstraete I.;
RT   "Conversion of methionine to cysteine in Bacillus subtilis and its
RT   regulation.";
RL   J. Bacteriol. 189:187-197(2007).
RN   [7]
RP   FUNCTION AS A REGULATOR OF CYMR ACTIVITY, INDUCTION, SUBUNIT, AND
RP   INTERACTION WITH CYMR.
RC   STRAIN=168;
RX   PubMed=18974048; DOI=10.1074/jbc.m805951200;
RA   Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P.,
RA   Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I.;
RT   "The CymR regulator in complex with the enzyme CysK controls cysteine
RT   metabolism in Bacillus subtilis.";
RL   J. Biol. Chem. 283:35551-35560(2008).
CC   -!- FUNCTION: Catalyzes the conversion of O-acetylserine to cysteine. Also
CC       acts as a sensor of cysteine availability in the signal transduction
CC       pathway modulating CymR activity. When cysteine is present, the pool of
CC       O-acetylserine (OAS) is low, which leads to the formation of a CymR-
CC       CysK complex and transcriptional repression of the CymR regulon occurs.
CC       In the absence of cysteine, the OAS pool is high and the CymR-CysK
CC       complex is mostly dissociated, leading to a faster dissociation of CymR
CC       from its DNA targets and the lifting of CymR-dependent repression.
CC       {ECO:0000269|PubMed:18974048}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000269|PubMed:17056751};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer. Forms CymR(2):CysK(2) or CymR(4):CysK(4) complexes
CC       in the absence of O-acetylserine. {ECO:0000269|PubMed:18974048}.
CC   -!- INDUCTION: Highly expressed in the presence of methionine, but poorly
CC       expressed in the presence of cystine. Also induced by superoxide.
CC       Repressed both by sulfate and cysteine. {ECO:0000269|PubMed:11445163,
CC       ECO:0000269|PubMed:18974048}.
CC   -!- DISRUPTION PHENOTYPE: Grows very slowly with sulfate, butanesulfonate
CC       or cystine as sole sulfur source. {ECO:0000269|PubMed:11445163,
CC       ECO:0000269|PubMed:17056751}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
DR   EMBL; D26185; BAA05308.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11849.1; -; Genomic_DNA.
DR   PIR; S66103; S66103.
DR   RefSeq; NP_387954.1; NC_000964.3.
DR   RefSeq; WP_003244491.1; NZ_JNCM01000028.1.
DR   SMR; P37887; -.
DR   IntAct; P37887; 1.
DR   MINT; P37887; -.
DR   STRING; 224308.BSU00730; -.
DR   MoonProt; P37887; -.
DR   jPOST; P37887; -.
DR   PaxDb; P37887; -.
DR   PRIDE; P37887; -.
DR   EnsemblBacteria; CAB11849; CAB11849; BSU00730.
DR   GeneID; 936636; -.
DR   KEGG; bsu:BSU00730; -.
DR   PATRIC; fig|224308.179.peg.73; -.
DR   eggNOG; ENOG4105C6T; Bacteria.
DR   eggNOG; COG0031; LUCA.
DR   HOGENOM; HOG000217394; -.
DR   InParanoid; P37887; -.
DR   KO; K01738; -.
DR   OMA; WDSGERY; -.
DR   PhylomeDB; P37887; -.
DR   BioCyc; BSUB:BSU00730-MONOMER; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:CAFA.
DR   GO; GO:0004124; F:cysteine synthase activity; IDA:CAFA.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IPI:CAFA.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:CAFA.
DR   GO; GO:0009087; P:methionine catabolic process; IMP:CAFA.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR   GO; GO:1904798; P:positive regulation of core promoter binding; IDA:CAFA.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:CAFA.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01139; cysK; 1.
DR   TIGRFAMs; TIGR01136; cysKM; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37887.
DR   SWISS-2DPAGE; P37887.
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Direct protein sequencing;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8755892,
FT                   ECO:0000269|PubMed:9298659"
FT   CHAIN           2..308
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167081"
FT   REGION          179..183
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  32820 MW;  79350923DF2B73CA CRC64;
     MVRVANSITE LIGNTPIVKL NRLADENSAD VYLKLEYMNP GSSVKDRIGL AMIEAAEKEG
     KLKAGNTIIE PTSGNTGIGL AMVAAAKGLK AILVMPDTMS MERRNLLRAY GAELVLTPGA
     EGMKGAIKKA EELAEKHGYF VPQQFNNPSN PEIHRQTTGK EIVEQFGDDQ LDAFVAGIGT
     GGTITGAGEV LKEAYPSIKI YAVEPSDSPV LSGGKPGPHK IQGIGAGFVP DILNTEVYDE
     IFPVKNEEAF EYARRAAREE GILGGISSGA AIYAALQVAK KLGKGKKVLA IIPSNGERYL
     STPLYQFD
//

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