CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010030
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent zinc metalloprotease FtsH 
Protein Synonyms/Alias
  
Gene Name
 ftsH 
Gene Synonyms/Alias
 MPN_671; MP171 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
315RVRDLFNKAKKAAPCacetylation[1]
419KNKNLSSKISLLDVAacetylation[1]
606GTVPPGTKLFSEQTAacetylation[1]
668DYIHEHTKLPPEILAacetylation[1]
692KAEAKEAKLNKKTEKacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
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 (By similarity). 
Sequence Annotation
 NP_BIND 268 275 ATP (Potential).
 ACT_SITE 491 491 By similarity.
 METAL 490 490 Zinc; catalytic (By similarity).
 METAL 494 494 Zinc; catalytic (By similarity).
 METAL 569 569 Zinc; catalytic (By similarity).  
Keyword
 ATP-binding; 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
 709 AA 
Protein Sequence
MKKNKGLNEA TTSEKPQFPK RTAWKIFWWV VILAIIIGIL VYILMPRATT AVIEKWELSG 60
TTLSAQIKGL SGKHTFQRIN NSTYVTDDIL QVSISFQGIN PIVVTAHKAT NGSGETIFNI 120
ANLSINQSTG KAIVNGMMTQ DQKSNNGTEL ASIKGLHDIG TFVAPDTRAR DVLNIFFGLL 180
PIIIFVIFFL LFWRSARGIS GGGRSEEDNI FSIGKTQAKL AKSSVRFDNI AGLQEEKHEL 240
LEIVDYLKNP LKYAQMGARS PRGVILYGPP GTGKTLLAKA VAGEAGVPFF QSTGSGFEDM 300
LVGVGAKRVR DLFNKAKKAA PCIIFIDEID SVGSKRGRVE LSSYSVVEQT LNQLLAEMDG 360
FTSRTGVVVM AATNRLDVLD DALLRPGRFD RHIQINLPDI KEREGILQVH AKNKNLSSKI 420
SLLDVAKRTP GFSGAQLENV INEATLLAVR DNRTTINMND IDEAIDRVIA GPAKKSRVVS 480
DADRKLVAYH EAGHALVGLH VHSNDEVQKI TIIPRGQAGG YTLSTPKSGD LNLKRKSDLL 540
AMIATAMGGR AAEEEIYGPL EITTGASSDF YKATNIARAM VTQLGMSKLG QVQYVPSQGT 600
VPPGTKLFSE QTAKDIDFEI NAIIEEQYKK ARTIIKTNRK ELELLVEALL IAETILKSDI 660
DYIHEHTKLP PEILAQKQEQ QAKQKAEAKE AKLNKKTEKD TEKDSETNS 709 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0016887; F:ATPase activity; IEA:HAMAP.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0030163; P:protein catabolic process; IEA:HAMAP.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
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