Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A6Q6 (FABZ_ECOLI)

Last modified November 3, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase
      Short name=(3R)-hydroxymyristoyl ACP dehydrase
    EC=4.2.1.-
Alternative name(s):
    17 kDa actomyosin component
Gene names
Name: fabZ
Synonyms: sefA, yaeA
Ordered Locus Names: b0180, JW0175
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in saturated fatty acids biosynthesis. Ref.7 Ref.8

Subunit structure

Oligomer. HAMAP MF_00406

Subcellular location

Cytoplasm. HAMAP MF_00406

Post-translational modification

The N-terminus is blocked. HAMAP MF_00406

Sequence similarities

Belongs to the thioester dehydratase family. FabZ subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: InterPro

lipid A biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydro-lyase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase HAMAP MF_00406
PRO_0000091673

Sites

Active site541 By similarity

Experimental info

Sequence conflict140 – 1412EA → DR Ref.1
Sequence conflict150 – 1512EA → RRDT Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A6Q6-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 91F514A7319C2FB1

FASTA15117,033
        10         20         30         40         50         60 
MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI 

        70         80         90        100        110        120 
FPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT 

       130        140        150 
RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A 

« Hide

References

« Hide 'large scale' references
[1]"First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene."
Coleman J., Raetz C.R.H.
J. Bacteriol. 170:1268-1274(1988) [PubMed: 3277952] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Coleman J.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110."
Foster S.J.
FEMS Microbiol. Lett. 110:295-298(1993) [PubMed: 8354462] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18, SIMILARITY, POSSIBLE FUNCTION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis."
Mohan S., Kelly T.M., Eveland S.S., Raetz C.R.H., Anderson M.S.
J. Biol. Chem. 269:32896-32903(1994) [PubMed: 7806516] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

M19334 Genomic DNA. Translation: AAC36917.1.
U00096 Genomic DNA. Translation: AAC73291.1.
AP009048 Genomic DNA. Translation: BAA77855.1.
U70214 Genomic DNA. Translation: AAB08609.1.
PIRD64742.
RefSeqAP_000840.1.
NP_414722.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP0A6Q6.

Genome annotation databases

GeneID944888.
GenomeReviewsGene locus JW0175 in contig AP009048_GR.
Gene locus b0180 in contig U00096_GR.
KEGGecj:JW0175.
eco:b0180.

Organism-specific databases

EchoBASEEB1261.
EcoGeneEG11284. fabZ.
CMRSearch...

Phylogenomic databases

HOGENOMP0A6Q6.
OMAEFIKERR.

Enzyme and pathway databases

BioCycEcoCyc:FABZ-MON.
MetaCyc:FABZ-MON.

Gene expression databases

GenevestigatorP0A6Q6.

Family and domain databases

HAMAPMF_00406.
[Tree]
InterProIPR013114. FabA_FabZ.
IPR010084. FabZ.
[Graphical view]
PfamPF07977. FabA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01750. fabZ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABZ_ECOLI
AccessionPrimary (citable) accession number: P0A6Q6
Secondary accession number(s): P21774
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents