Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Uncharacterized carboxylesterase nap

Gene

nap

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei130Transition state stabilizerBy similarity1
Active sitei274Proton acceptorBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciBSUB:BSU05440-MONOMER.

Protein family/group databases

ESTHERibacsu-cbxnp. 6_AlphaBeta_hydrolase.

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized carboxylesterase nap (EC:3.1.1.1)
Gene namesi
Name:nap
Ordered Locus Names:BSU05440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003608161 – 300Uncharacterized carboxylesterase napAdd BLAST300

Proteomic databases

PaxDbiP96688.
PRIDEiP96688.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003063.

Structurei

Secondary structure

1300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 26Combined sources14
Beta strandi34 – 38Combined sources5
Beta strandi43 – 51Combined sources9
Beta strandi57 – 61Combined sources5
Turni64 – 66Combined sources3
Helixi68 – 71Combined sources4
Turni72 – 74Combined sources3
Helixi75 – 81Combined sources7
Beta strandi82 – 87Combined sources6
Beta strandi92 – 95Combined sources4
Helixi105 – 118Combined sources14
Beta strandi122 – 129Combined sources8
Helixi131 – 142Combined sources12
Helixi144 – 146Combined sources3
Beta strandi147 – 154Combined sources8
Beta strandi156 – 158Combined sources3
Helixi164 – 171Combined sources8
Turni172 – 174Combined sources3
Helixi178 – 186Combined sources9
Turni187 – 189Combined sources3
Helixi195 – 206Combined sources12
Beta strandi209 – 211Combined sources3
Beta strandi220 – 222Combined sources3
Helixi227 – 231Combined sources5
Beta strandi237 – 242Combined sources6
Helixi250 – 260Combined sources11
Beta strandi265 – 269Combined sources5
Helixi276 – 279Combined sources4
Helixi281 – 292Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R11X-ray1.96A/B/C/D1-294[»]
ProteinModelPortaliP96688.
SMRiP96688.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96688.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiENOG4108WC5. Bacteria.
COG0596. LUCA.
HOGENOMiHOG000091205.
InParanoidiP96688.
OMAiSSTMWYP.
PhylomeDBiP96688.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P96688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNHSSSIPE LSDNGIRYYQ TYNESLSLWP VRCKSFYIST RFGQTHVIAS
60 70 80 90 100
GPEDAPPLVL LHGALFSSTM WYPNIADWSS KYRTYAVDII GDKNKSIPEN
110 120 130 140 150
VSGTRTDYAN WLLDVFDNLG IEKSHMIGLS LGGLHTMNFL LRMPERVKSA
160 170 180 190 200
AILSPAETFL PFHHDFYKYA LGLTASNGVE TFLNWMMNDQ NVLHPIFVKQ
210 220 230 240 250
FKAGVMWQDG SRNPNPNADG FPYVFTDEEL RSARVPILLL LGEHEVIYDP
260 270 280 290 300
HSALHRASSF VPDIEAEVIK NAGHVLSMEQ PTYVNERVMR FFNAETGISR
Length:300
Mass (Da):33,953
Last modified:May 1, 1997 - v1
Checksum:iFA818689172007AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19378.1.
AL009126 Genomic DNA. Translation: CAB12351.1.
PIRiC69664.
RefSeqiNP_388425.1. NC_000964.3.
WP_003242638.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12351; CAB12351; BSU05440.
GeneIDi938069.
KEGGibsu:BSU05440.
PATRICi18972694. VBIBacSub10457_0568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19378.1.
AL009126 Genomic DNA. Translation: CAB12351.1.
PIRiC69664.
RefSeqiNP_388425.1. NC_000964.3.
WP_003242638.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R11X-ray1.96A/B/C/D1-294[»]
ProteinModelPortaliP96688.
SMRiP96688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003063.

Protein family/group databases

ESTHERibacsu-cbxnp. 6_AlphaBeta_hydrolase.

Proteomic databases

PaxDbiP96688.
PRIDEiP96688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12351; CAB12351; BSU05440.
GeneIDi938069.
KEGGibsu:BSU05440.
PATRICi18972694. VBIBacSub10457_0568.

Phylogenomic databases

eggNOGiENOG4108WC5. Bacteria.
COG0596. LUCA.
HOGENOMiHOG000091205.
InParanoidiP96688.
OMAiSSTMWYP.
PhylomeDBiP96688.

Enzyme and pathway databases

BioCyciBSUB:BSU05440-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP96688.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNAP_BACSU
AccessioniPrimary (citable) accession number: P96688
Secondary accession number(s): Q797G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.