SCMP_BACSU
ID SCMP_BACSU Reviewed; 380 AA.
AC P54955;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N-acetylcysteine deacetylase {ECO:0000303|PubMed:29626092};
DE EC=3.5.1.- {ECO:0000305|PubMed:29626092};
DE AltName: Full=S-(2-succino)cysteine metabolism operon protein P {ECO:0000303|PubMed:29626092};
GN Name=scmP {ECO:0000303|PubMed:29626092};
GN Synonyms=sndB {ECO:0000303|PubMed:29626092}, yxeP;
GN OrderedLocusNames=BSU39470; ORFNames=LP9H;
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 / BGSC1A1;
RX PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT between the iol and hut operons.";
RL DNA Res. 2:295-301(1995).
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 SEQUENCE REVISION TO 54 AND 194.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=168;
RX PubMed=29626092; DOI=10.1074/jbc.ra118.002925;
RA Niehaus T.D., Folz J., McCarty D.R., Cooper A.J.L., Moraga Amador D.,
RA Fiehn O., Hanson A.D.;
RT "Identification of a metabolic disposal route for the oncometabolite S-(2-
RT succino)cysteine in Bacillus subtilis.";
RL J. Biol. Chem. 293:8255-8263(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH NICKEL, AND
RP COFACTOR.
RA Minasov G., Shuvalova L., Brunzelle J.S., Collart F.R., Anderson W.F.;
RT "Structure of Bacillus subtilis YxeP protein, a dinuclear metal binding
RT peptidase from M20 family.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Probably catalyzes the deacetylation of N-acetylcysteine
CC (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine
CC (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a
CC sole sulfur source, via its metabolization to cysteine.
CC {ECO:0000269|PubMed:29626092}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305|Ref.5};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|Ref.5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC {ECO:0000305|PubMed:29626092}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not lose the ability
CC to grow on 2SC as the sulfur source because of the presence of other
CC deacetylases that can compensate for scmP (yxeP) deficiency. In a
CC triple mutant lacking this gene, ytnL and yhaA, the levels of NAC
CC highly increases after addition of 2SC. {ECO:0000269|PubMed:29626092}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; D45912; BAA08332.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15983.2; -; Genomic_DNA.
DR PIR; B70076; B70076.
DR RefSeq; NP_391826.2; NC_000964.3.
DR RefSeq; WP_003243840.1; NZ_JNCM01000034.1.
DR PDB; 1YSJ; X-ray; 2.40 A; A/B=1-380.
DR PDBsum; 1YSJ; -.
DR AlphaFoldDB; P54955; -.
DR SMR; P54955; -.
DR STRING; 224308.BSU39470; -.
DR MEROPS; M20.015; -.
DR PaxDb; P54955; -.
DR PRIDE; P54955; -.
DR DNASU; 937572; -.
DR EnsemblBacteria; CAB15983; CAB15983; BSU_39470.
DR GeneID; 937572; -.
DR KEGG; bsu:BSU39470; -.
DR PATRIC; fig|224308.179.peg.4272; -.
DR eggNOG; COG1473; Bacteria.
DR InParanoid; P54955; -.
DR OMA; EWHHPAF; -.
DR PhylomeDB; P54955; -.
DR BioCyc; BSUB:BSU39470-MON; -.
DR BioCyc; MetaCyc:BSU39470-MON; -.
DR UniPathway; UPA00136; -.
DR EvolutionaryTrace; P54955; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis; Hydrolase;
KW Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..380
FT /note="N-acetylcysteine deacetylase"
FT /id="PRO_0000061962"
FT BINDING 98
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 98
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 100
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 134
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 158
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 350
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.5"
FT CONFLICT 54
FT /note="G -> A (in Ref. 1; BAA08332)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="G -> S (in Ref. 1; BAA08332)"
FT /evidence="ECO:0000305"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1YSJ"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:1YSJ"
FT TURN 145..150
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 258..278
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:1YSJ"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1YSJ"
FT HELIX 360..378
FT /evidence="ECO:0007829|PDB:1YSJ"
SQ SEQUENCE 380 AA; 41552 MW; F36EAC6EF01AAFD3 CRC64;
MADKAFHTRL INMRRDLHEH PELSFQEVET TKKIRRWLEE EQIEILDVPQ LKTGVIAEIK
GREDGPVIAI RADIDALPIQ EQTNLPFASK VDGTMHACGH DFHTASIIGT AMLLNQRRAE
LKGTVRFIFQ PAEEIAAGAR KVLEAGVLNG VSAIFGMHNK PDLPVGTIGV KEGPLMASVD
RFEIVIKGKG GHAGIPNNSI DPIAAAGQII SGLQSVVSRN ISSLQNAVVS ITRVQAGTSW
NVIPDQAEME GTVRTFQKEA RQAVPEHMRR VAEGIAAGYG AQAEFKWFPY LPSVQNDGTF
LNAASEAAAR LGYQTVHAEQ SPGGEDFALY QEKIPGFFVW MGTNGTEEWH HPAFTLDEEA
LTVASQYFAE LAVIVLETIK
