UniProtKB - P54955 (SCMP_BACSU)
Protein
N-acetylcysteine deacetylase
Gene
scmP
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine.1 Publication
Cofactori
a divalent metal cation1 PublicationNote: Binds 2 divalent metal cations per subunit.1 Publication
: L-cysteine biosynthesis Pathwayi
This protein is involved in the pathway L-cysteine biosynthesis, which is part of Amino-acid biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 98 | Nickel 11 Publication | 1 | |
Metal bindingi | 98 | Nickel 21 Publication | 1 | |
Metal bindingi | 100 | Nickel 2; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 134 | Nickel 11 Publication | 1 | |
Metal bindingi | 158 | Nickel 21 Publication | 1 | |
Metal bindingi | 350 | Nickel 11 Publication | 1 |
GO - Molecular functioni
- hydrolase activity Source: GO_Central
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- cysteine biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Hydrolase |
Biological process | Amino-acid biosynthesis, Cysteine biosynthesis |
Ligand | Metal-binding, Nickel |
Enzyme and pathway databases
BioCyci | BSUB:BSU39470-MONOMER |
UniPathwayi | UPA00136 |
Protein family/group databases
MEROPSi | M20.015 |
Names & Taxonomyi
Protein namesi | Recommended name: N-acetylcysteine deacetylase1 Publication (EC:3.5.1.-1 Publication)Alternative name(s): S-(2-succino)cysteine metabolism operon protein P1 Publication |
Gene namesi | Name:scmP1 Publication Synonyms:sndB1 Publication, yxeP Ordered Locus Names:BSU39470 ORF Names:LP9H |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene do not lose the ability to grow on 2SC as the sulfur source because of the presence of other deacetylases that can compensate for scmP (yxeP) deficiency. In a triple mutant lacking this gene, ytnL and yhaA, the levels of NAC highly increases after addition of 2SC.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000061962 | 1 – 380 | N-acetylcysteine deacetylaseAdd BLAST | 380 |
Proteomic databases
PaxDbi | P54955 |
PRIDEi | P54955 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P54955 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P54955 |
Family & Domainsi
Sequence similaritiesi
Belongs to the peptidase M20 family.Curated
Phylogenomic databases
eggNOGi | COG1473, Bacteria |
InParanoidi | P54955 |
OMAi | EWHHPAF |
PhylomeDBi | P54955 |
Family and domain databases
InterProi | View protein in InterPro IPR017439, Amidohydrolase IPR036264, Bact_exopeptidase_dim_dom IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
PIRSFi | PIRSF005962, Pept_M20D_amidohydro, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01891, amidohydrolases, 1 hit |
i Sequence
Sequence statusi: Complete.
P54955-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MADKAFHTRL INMRRDLHEH PELSFQEVET TKKIRRWLEE EQIEILDVPQ
60 70 80 90 100
LKTGVIAEIK GREDGPVIAI RADIDALPIQ EQTNLPFASK VDGTMHACGH
110 120 130 140 150
DFHTASIIGT AMLLNQRRAE LKGTVRFIFQ PAEEIAAGAR KVLEAGVLNG
160 170 180 190 200
VSAIFGMHNK PDLPVGTIGV KEGPLMASVD RFEIVIKGKG GHAGIPNNSI
210 220 230 240 250
DPIAAAGQII SGLQSVVSRN ISSLQNAVVS ITRVQAGTSW NVIPDQAEME
260 270 280 290 300
GTVRTFQKEA RQAVPEHMRR VAEGIAAGYG AQAEFKWFPY LPSVQNDGTF
310 320 330 340 350
LNAASEAAAR LGYQTVHAEQ SPGGEDFALY QEKIPGFFVW MGTNGTEEWH
360 370 380
HPAFTLDEEA LTVASQYFAE LAVIVLETIK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 54 | G → A in BAA08332 (PubMed:8867804).Curated | 1 | |
Sequence conflicti | 194 | G → S in BAA08332 (PubMed:8867804).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45912 Genomic DNA Translation: BAA08332.1 AL009126 Genomic DNA Translation: CAB15983.2 |
PIRi | B70076 |
RefSeqi | NP_391826.2, NC_000964.3 WP_003243840.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB15983; CAB15983; BSU39470 |
GeneIDi | 937572 |
KEGGi | bsu:BSU39470 |
PATRICi | fig|224308.179.peg.4272 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45912 Genomic DNA Translation: BAA08332.1 AL009126 Genomic DNA Translation: CAB15983.2 |
PIRi | B70076 |
RefSeqi | NP_391826.2, NC_000964.3 WP_003243840.1, NZ_JNCM01000034.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1YSJ | X-ray | 2.40 | A/B | 1-380 | [»] | |
SMRi | P54955 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU39470 |
Protein family/group databases
MEROPSi | M20.015 |
Proteomic databases
PaxDbi | P54955 |
PRIDEi | P54955 |
Protocols and materials databases
DNASUi | 937572 |
Genome annotation databases
EnsemblBacteriai | CAB15983; CAB15983; BSU39470 |
GeneIDi | 937572 |
KEGGi | bsu:BSU39470 |
PATRICi | fig|224308.179.peg.4272 |
Phylogenomic databases
eggNOGi | COG1473, Bacteria |
InParanoidi | P54955 |
OMAi | EWHHPAF |
PhylomeDBi | P54955 |
Enzyme and pathway databases
UniPathwayi | UPA00136 |
BioCyci | BSUB:BSU39470-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P54955 |
Family and domain databases
InterProi | View protein in InterPro IPR017439, Amidohydrolase IPR036264, Bact_exopeptidase_dim_dom IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
PIRSFi | PIRSF005962, Pept_M20D_amidohydro, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01891, amidohydrolases, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SCMP_BACSU | |
Accessioni | P54955Primary (citable) accession number: P54955 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | July 28, 2009 | |
Last modified: | December 2, 2020 | |
This is version 135 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries