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Protein

ATP-dependent zinc metalloprotease FtsH

Gene

ftsH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.
As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).

Miscellaneous

The ftsH gene was discovered independently through 3 different phenotypes and received 3 different names: ftsH, for filamentous temperature-sensitive; tolZ, for colicin tolerance, and hlfB, because mutants show a high frequency of lysogenization when infected with phage lambda.1 Publication
Requires ATP for protease catalytic activity, probably due to tight coupling of the 2 activities; ADP or non-hydrolyzable analogs cannot substitute, except when unfolded, non-physiological substrates are tested.

Caution

Glu-476 was identified as the third Zn ligand (PubMed:11827531), however in other crystal structures (Aquifex aeolicus and Thermotoga maritima) the conserved equivalent residue does not bind Zn. Instead it makes a hydrogen bond with the side chain of the first catalytic Zn-binding residue and indirectly stabilizes the Zn.1 Publication

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

(Microbial infection) Activity against phage lambda cII protein is inhibited by EDTA but not by PMSF. In vitro pre-incubation of FtsH with HflKC abolishes its activity against phage lambda cII protein at the cytoplasmic side of the membrane.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei225Substrate bindingCurated1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi414Zinc; catalyticCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei415Curated1
Metal bindingi418Zinc; catalyticCurated1
Metal bindingi492Zinc; catalyticUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi192 – 199ATPUniRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • protein catabolic process Source: GO_Central
  • proteolysis Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11506-MONOMER
MetaCyc:EG11506-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.B17 2026
3.4.24.B20 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0AAI3

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M41.001

Transport Classification Database

More...
TCDBi
9.B.307.1.2 the ftsh aaa(+) zinc metaloprotease (ftsh) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP-dependent zinc metalloprotease FtsHUniRule annotation (EC:3.4.24.-UniRule annotation)
Alternative name(s):
Cell division protease FtsH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ftsHUniRule annotation
Synonyms:hflB, mrsC, std, tolZ
Ordered Locus Names:b3178, JW3145
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG11506 ftsH

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4Cytoplasmic1 Publication4
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei5 – 25HelicalCuratedAdd BLAST21
Topological domaini26 – 98Periplasmic1 PublicationAdd BLAST73
Transmembranei99 – 119HelicalCuratedAdd BLAST21
Topological domaini120 – 644Cytoplasmic1 PublicationAdd BLAST525

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Lethality, due to increased levels of LpxC, which increases the level of LPS in the cell and results in formation of abnormal membrane structures in the periplasm. Lethality is suppressed under conditions in which LPS synthesis is reduced.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi201L → N: No in vivo protease activity, no in vitro ATPase activity. 1 Publication1
Mutagenesisi225F → A, D, E, G, N, Q, R, S or T: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo. 1 Publication1
Mutagenesisi225F → C or H: Partially complements ftsH1 at 42 degrees Celsius, some protease activity in vivo. 1 Publication1
Mutagenesisi225F → I, L, M, V, W or Y: Complements ftsH1 at 42 degrees Celsius, restores protease activity in vivo. 1 Publication1
Mutagenesisi227G → A: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo. 1 Publication1
Mutagenesisi297T → A: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius. 1 Publication1
Mutagenesisi298N → A: No in vivo protease activity. 1 Publication1
Mutagenesisi304D → A or N: No in vivo protease activity, no in vitro ATPase activity; probably still binds ATP. 1 Publication1
Mutagenesisi304D → E: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius. 1 Publication1
Mutagenesisi307L → A: Low protease activity in vivo. 1 Publication1
Mutagenesisi309R → A, L or K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP. 1 Publication1
Mutagenesisi312R → A, L or K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP. 1 Publication1
Mutagenesisi414 – 418HEAGH → KEAGK: Loss of protease function. 5
Mutagenesisi414H → Y: Loss of protease function. 1 Publication1
Mutagenesisi415E → Q: Loss of protease activity in vivo. 1 Publication1
Mutagenesisi418H → Y in tolZ21; loss of protease function in vivo, retains about 25% ATPase activity, temperature sensitive. 2 Publications1
Mutagenesisi463E → K in ftsH1; a temperature-sensitive mutant which increases the frequency of lysogenization of phage lambda; when associated with A-587. 1 Publication1
Mutagenesisi476E → D, K or V: Severe loss of protease function that is restored by excess Zn. 1 Publication1
Mutagenesisi476E → Q: Little effect on protease function. 1 Publication1
Mutagenesisi536H → R in hflB29; increases the frequency of lysogenization of phage lambda. 1 Publication1
Mutagenesisi582E → D, K or Q: No effect on protease function. 1 Publication1
Mutagenesisi582E → V: Decreased protease function. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000846311 – 644ATP-dependent zinc metalloprotease FtsHAdd BLAST644

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AAI3

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0AAI3

PRoteomics IDEntifications database

More...
PRIDEi
P0AAI3

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The E.coli AAA domain has been modeled as a homohexamer, in Thermus thermophilus the same domain crystallizes as a homohexamer. Forms a complex with HflKC (formerly called HflA); complex formation is stimulated by ATP. Interacts with YccA, and probably weakly with QmcA. Can be cross-linked to YidC (OxaA) and to a nascent polypeptide chain for an integral membrane protein.4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262980, 385 interactors

Database of interacting proteins

More...
DIPi
DIP-35828N

Protein interaction database and analysis system

More...
IntActi
P0AAI3, 28 interactors

Molecular INTeraction database

More...
MINTi
P0AAI3

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3352

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0AAI3

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0AAI3

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AAI3

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the central section; belongs to the AAA ATPase family.UniRule annotation
In the C-terminal section; belongs to the peptidase M41 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C3H Bacteria
COG0465 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000217276

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AAI3

KEGG Orthology (KO)

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KOi
K03798

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AAI3

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01458 FtsH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR005936 FtsH
IPR027417 P-loop_NTPase
IPR011546 Pept_M41_FtsH_extracell
IPR000642 Peptidase_M41
IPR037219 Peptidase_M41-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF06480 FtsH_ext, 1 hit
PF01434 Peptidase_M41, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF140990 SSF140990, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01241 FtsH_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00674 AAA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0AAI3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNNDQVREAR
60 70 80 90 100
INGREINVTK KDSNRYTTYI PVQDPKLLDN LLTKNVKVVG EPPEEPSLLA
110 120 130 140 150
SIFISWFPML LLIGVWIFFM RQMQGGGGKG AMSFGKSKAR MLTEDQIKTT
160 170 180 190 200
FADVAGCDEA KEEVAELVEY LREPSRFQKL GGKIPKGVLM VGPPGTGKTL
210 220 230 240 250
LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA KKAAPCIIFI
260 270 280 290 300
DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP
310 320 330 340 350
DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL APDIDAAIIA
360 370 380 390 400
RGTPGFSGAD LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS
410 420 430 440 450
MVMTEAQKES TAYHEAGHAI IGRLVPEHDP VHKVTIIPRG RALGVTFFLP
460 470 480 490 500
EGDAISASRQ KLESQISTLY GGRLAEEIIY GPEHVSTGAS NDIKVATNLA
510 520 530 540 550
RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE TARIIDQEVK
560 570 580 590 600
ALIERNYNRA RQLLTDNMDI LHAMKDALMK YETIDAPQID DLMARRDVRP
610 620 630 640
PAGWEEPGAS NNSGDNGSPK APRPVDEPRT PNPGNTMSEQ LGDK
Length:644
Mass (Da):70,708
Last modified:October 11, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE24A753D8F486CA1
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA97508 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M83138 Genomic DNA Translation: AAA23813.1
U01376 Genomic DNA Translation: AAA97508.1 Different initiation.
U18997 Genomic DNA Translation: AAA57979.1
U00096 Genomic DNA Translation: AAC76210.1
AP009048 Genomic DNA Translation: BAE77222.1

Protein sequence database of the Protein Information Resource

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PIRi
S35109

NCBI Reference Sequences

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RefSeqi
NP_417645.1, NC_000913.3
WP_001107467.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76210; AAC76210; b3178
BAE77222; BAE77222; BAE77222

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947690

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3145
eco:b3178

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3271

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83138 Genomic DNA Translation: AAA23813.1
U01376 Genomic DNA Translation: AAA97508.1 Different initiation.
U18997 Genomic DNA Translation: AAA57979.1
U00096 Genomic DNA Translation: AAC76210.1
AP009048 Genomic DNA Translation: BAE77222.1
PIRiS35109
RefSeqiNP_417645.1, NC_000913.3
WP_001107467.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LV7X-ray1.50A141-395[»]
4V0BX-ray2.55A/B/C25-96[»]
ProteinModelPortaliP0AAI3
SMRiP0AAI3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262980, 385 interactors
DIPiDIP-35828N
IntActiP0AAI3, 28 interactors
MINTiP0AAI3
STRINGi316385.ECDH10B_3352

Protein family/group databases

MEROPSiM41.001
TCDBi9.B.307.1.2 the ftsh aaa(+) zinc metaloprotease (ftsh) family

Proteomic databases

EPDiP0AAI3
PaxDbiP0AAI3
PRIDEiP0AAI3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76210; AAC76210; b3178
BAE77222; BAE77222; BAE77222
GeneIDi947690
KEGGiecj:JW3145
eco:b3178
PATRICifig|511145.12.peg.3271

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1469
EcoGeneiEG11506 ftsH

Phylogenomic databases

eggNOGiENOG4105C3H Bacteria
COG0465 LUCA
HOGENOMiHOG000217276
InParanoidiP0AAI3
KOiK03798
PhylomeDBiP0AAI3

Enzyme and pathway databases

BioCyciEcoCyc:EG11506-MONOMER
MetaCyc:EG11506-MONOMER
BRENDAi3.4.24.B17 2026
3.4.24.B20 2026
SABIO-RKiP0AAI3

Miscellaneous databases

EvolutionaryTraceiP0AAI3

Protein Ontology

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PROi
PR:P0AAI3

Family and domain databases

HAMAPiMF_01458 FtsH, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR005936 FtsH
IPR027417 P-loop_NTPase
IPR011546 Pept_M41_FtsH_extracell
IPR000642 Peptidase_M41
IPR037219 Peptidase_M41-like
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF06480 FtsH_ext, 1 hit
PF01434 Peptidase_M41, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF140990 SSF140990, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01241 FtsH_fam, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFTSH_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AAI3
Secondary accession number(s): P28691, Q2M934
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: December 5, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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