Reviewed, UniProtKB/Swiss-Prot P0A9M1 (LON_ECOL6)

Names and origin

Protein names

Recommended name:
    ATP-dependent protease La
    EC=3.4.21.53

Gene names

Name:	lon
Ordered Locus Names:	c0555

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Degrades short-lived regulatory and abnormal proteins in presence of ATP. Degrades the regulatory proteins rcsA and sulA. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate. Its overproduction specifically inhibits translation trough at least two different pathways, one of them being the yoeB-yefM toxin-antitoxin system By similarity.
Catalytic activity	Hydrolysis of proteins in presence of ATP.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase S16 family. Contains 1 Lon domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent peptidase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase 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 – 784	784	ATP-dependent protease La		PRO_0000076134
Regions
	Domain	10 – 202	193	Lon
	Nucleotide binding	356 – 363	8	ATP Potential
	Compositional bias	211 – 219	9	Arg/Lys-rich (basic)
	Compositional bias	240 – 252	13	Asp/Glu-rich (acidic)
	Compositional bias	255 – 270	16	Arg/Lys-rich (basic)
Sites
	Active site	679	1	By similarity
	Active site	722	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9M1-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 4042499C97694EF8	FASTA	784	87,438
	10 20 30 40 50 60 MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST 70 80 90 100 110 120 DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP 130 140 150 160 170 180 TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK 190 200 210 220 230 240 QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE 250 260 270 280 290 300 LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ 310 320 330 340 350 360 VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV 370 380 390 400 410 420 GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF 430 440 450 460 470 480 LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP 490 500 510 520 530 540 LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG 550 560 570 580 590 600 VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG 610 620 630 640 650 660 LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE 670 680 690 700 710 720 KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK 730 740 750 760 770 780 EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV VTAK

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN79033.1. Different initiation.
RefSeq	NP_752489.1.
3D structure databases
SMR	P0A9M1. Positions 8-117, 491-584, 594-784.
ModBase	Search...
Genome annotation databases
GeneID	1035203.
GenomeReviews	Gene locus c0555 in contig AE014075_GR.
KEGG	ecc:c0555.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A9M1.
OMA	P0A9M1. VMKESIQ.
Enzyme and pathway databases
BRENDA	3.4.21.53. 292881.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR008269. Pept_S16_C. IPR004815. Pept_S16_lon. IPR003111. Pept_S16_N. IPR008268. Peptidase_S16_AS. IPR001984. Peptidase_S16_C. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF02190. LON. 1 hit. PF05362. Lon_C. 1 hit. [Graphical view]
PRINTS	PR00830. ENDOLAPTASE.
SMART	SM00382. AAA. 1 hit. SM00464. LON. 1 hit. [Graphical view]
TIGRFAMs	TIGR00763. lon. 1 hit.
PROSITE	PS01046. LON_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LON_ECOL6

Accession

Primary (citable) accession number: P0A9M1
Secondary accession number(s): P08177, P78219

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 33 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)