P0A6Q6 (FABZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in saturated fatty acids biosynthesis. Ref.7 Ref.8
Subunit structure	Oligomer.
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 process	Lipid A biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro lipid A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydro-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase HAMAP MF_00406		PRO_0000091673
Sites
	Active site	54	1	By similarity
Experimental info
	Mutagenesis	85	1	L → P in sfhC21; suppresses an ftsH deletion mutant as well as an ftsH temperature-sensitive mutation. Probably stabilizes the enzyme. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P0A6Q6 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 91F514A7319C2FB1	FASTA	151	17,033
	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

References

	« Hide 'large scale' referencesShow '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 TO 140-141 AND 150-151.
[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.
[9]	"Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli." Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H., Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T., Matsuzawa H. Mol. Microbiol. 31:833-844(1999) [PubMed: 10048027] [Abstract] Cited for: MUTAGENESIS OF LEU-85. Strain: K12 / W3110 and W2252.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19334 Genomic DNA. Translation: AAC36917.1. U00096 Genomic DNA. Translation: AAC73291.1. AP009048 Genomic DNA. Translation: BAA77855.1. U70214 Genomic DNA. Translation: AAB08609.1.
PIR	D64742.
RefSeq	NP_414722.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A6Q6.
SMR	P0A6Q6. Positions 7-149.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31868N.
IntAct	P0A6Q6. 33 interactions.
MINT	MINT-1218564.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000625; EBESCP00000000625; EBESCG00000000519. EBESCT00000000626; EBESCP00000000626; EBESCG00000000519. EBESCT00000015256; EBESCP00000014547; EBESCG00000014316.
GeneID	944888.
GenomeReviews	Gene locus JW0175 in contig AP009048_GR. Gene locus b0180 in contig U00096_GR.
KEGG	ecj:JW0175. eco:b0180.
PATRIC	32115471. VBIEscCol129921_0187.
Organism-specific databases
EchoBASE	EB1261.
EcoGene	EG11284. fabZ.
Phylogenomic databases
eggNOG	COG0764.
GeneTree	EBGT00050000010796.
HOGENOM	HBG433282.
OMA	KERRGVA.
PhylomeDB	P0A6Q6.
ProtClustDB	PRK00006.
Enzyme and pathway databases
BioCyc	EcoCyc:FABZ-MONOMER. MetaCyc:FABZ-MONOMER.
Gene expression databases
Genevestigator	P0A6Q6.
Family and domain databases
HAMAP	MF_00406. FabZ. [Tree]
InterPro	IPR013114. FabA_FabZ. IPR010084. FabZ. [Graphical view]
KO	K02372.
Pfam	PF07977. FabA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01750. FabZ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABZ_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program