Reviewed, UniProtKB/Swiss-Prot P75942 (FLGJ_ECOLI)

Names and origin

Protein names

Recommended name:
    Peptidoglycan hydrolase flgJ
    EC=3.2.1.-
Alternative name(s):
    Muramidase flgJ

Gene names

Name:	flgJ
Synonyms:	fla FX, flaZ
Ordered Locus Names:	b1081, JW1068

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space By similarity.
Subcellular location	Periplasm By similarity.
Miscellaneous	Probably exported via the flagellum-specific export pathway.
Sequence similarities	In the N-terminal section; belongs to the flgJ family. In the C-terminal section; belongs to the glycosyl hydrolase 73 family.

Ontologies

Keywords
Biological process	Bacterial flagellum biogenesis Cell wall biogenesis/degradation
Cellular component	Periplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW ciliary or flagellar motility Inferred from electronic annotation. Source: InterPro flagellum assembly Inferred from electronic annotation. Source: InterPro peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	bacterial-type flagellum Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	amidase activity Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW motor 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 – 313	313	Peptidoglycan hydrolase flgJ		PRO_0000165705
Regions
	Region	148 – 313	166	Catalytic
Sites
	Active site	220	1	Potential
	Active site	245	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	P75942-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: C4B3CB8F36751CDF	FASTA	313	34,475
	10 20 30 40 50 60 MISDSKLLAS AAWDAQSLNE LKAKAGEDPA ANIRPVARQV EGMFVQMMLK SMRDALPKDG 70 80 90 100 110 120 LFSSEHTRLY TSMYDQQIAQ QMTAGKGLGL AEMMVKQMTP EQPLPEESTP AAPMKFPLET 130 140 150 160 170 180 VVRYQNQALS QLVQKAVPRN YDDSLPGDSK AFLAQLSLPA QLASQQSGVP HHLILAQAAL 190 200 210 220 230 240 ESGWGQRQIR RENGEPSYNL FGVKASGNWK GPVTEITTTE YENGEAKKVK AKFRVYSSYL 250 260 270 280 290 300 EALSDYVGLL TRNPRYAAVT TAASAEQGAQ ALQDAGYATD PHYARKLTNM IQQMKSISDK 310 VSKTYSMNID NLF

References

[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74165.1. AP009048 Genomic DNA. Translation: BAA35890.1.
PIR	F64851.
RefSeq	AP_001707.1. NP_415599.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P75942.
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Genome annotation databases
GeneID	947456.
GenomeReviews	Gene locus JW1068 in contig AP009048_GR. Gene locus b1081 in contig U00096_GR.
KEGG	ecj:JW1068. eco:b1081.
Organism-specific databases
EchoBASE	EB4020.
EcoGene	EG14272. flgJ.
CMR	Search...
Phylogenomic databases
eggNOG	COG3951.
HOGENOM	HBG336388.
OMA	SMRDANA.
Enzyme and pathway databases
BioCyc	EcoCyc:G366-MONOMER. ECOL168927:B1081-MONOMER.
Gene expression databases
Genevestigator	P75942.
Family and domain databases
InterPro	IPR013377. FlaG_FlgJ-2. IPR000423. Flag_FlgJ_1. IPR019301. Flagellar_prot_FlgJ_N. IPR013338. Lysozyme_dom_subfam2. IPR002901. Mano_Glyc_endo_b_GlcNAc. [Graphical view]
Pfam	PF01832. Glucosaminidase. 1 hit. PF10135. Rod-binding. 1 hit. [Graphical view]
PRINTS	PR01002. FLGFLGJ.
SMART	SM00047. LYZ2. 1 hit. [Graphical view]
TIGRFAMs	TIGR02541. flagell_FlgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FLGJ_ECOLI

Accession

Primary (citable) accession number: P75942

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	February 9, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)