UniProt Accession

 FTSH_ECOLI; P0AAI3; P28691; Q2M934 

Genbank Protein ID

 M83138; U01376; U18997; U00096; AP009048 

Genbank Nucleotide ID

 AAA23813.1; AAA97508.1; AAA57979.1; AAC76210.1; BAE77222.1 

Protein Name

 ATP-dependent zinc metalloprotease FtsH 

Protein Synonyms/Alias

 Cell division protease FtsH 

Gene Name

 ftsH 

Gene Synonyms/Alias

 hflB; mrsC; std; tolZ; b3178; JW3145 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
179	REPSRFQKLGGKIPK	acetylation	[1, 2]
203	TGKTLLAKAIAGEAK	acetylation	[2]
332	RGREQILKVHMRRVP	acetylation	[2]
387	VSMVEFEKAKDKIMM	acetylation	[2]
433	PEHDPVHKVTIIPRG	acetylation	[2]
550	RIIDQEVKALIERNY	acetylation	[2]
575	MDILHAMKDALMKYE	acetylation	[3]
580	AMKDALMKYETIDAP	acetylation	[2]

Reference

 [1] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 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, F(0) 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. 

Sequence Annotation

 NP_BIND 192 199 ATP (Potential).
 ACT_SITE 415 415 Probable.
 METAL 414 414 Zinc; catalytic (Probable).
 METAL 418 418 Zinc; catalytic (Probable).
 METAL 492 492 Zinc; catalytic (By similarity).  

Keyword

 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleotide-binding; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 644 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IDA:EcoliWiki.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0016887; F:ATPase activity; IDA:EcoliWiki.
 GO:0043273; F:CTPase activity; IDA:EcoliWiki.
 GO:0030145; F:manganese ion binding; IDA:EcoliWiki.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0030163; P:protein catabolic process; IEA:HAMAP.
 GO:0006508; P:proteolysis; IDA:EcoliWiki. 

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. 

Pfam

 PF00004; AAA
 PF06480; FtsH_ext
 PF01434; Peptidase_M41 

SMART

 SM00382; AAA 

PROSITE

 PS00674; AAA 

PRINTS