FTSH_MESCH
ID FTSH_MESCH Reviewed; 754 AA.
AC C5J6A7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=MCJ_003080;
OS Mesomycoplasma conjunctivae (strain ATCC 25834 / NCTC 10147 / HRC/581)
OS (Mycoplasma conjunctivae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=572263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25834 / NCTC 10147 / HRC/581;
RX PubMed=19534756; DOI=10.1186/1471-2105-10-s6-s7;
RA Calderon-Copete S.P., Wigger G., Wunderlin C., Schmidheini T., Frey J.,
RA Quail M.A., Falquet L.;
RT "The Mycoplasma conjunctivae genome sequencing, annotation and analysis.";
RL BMC Bioinformatics 10:S7-S7(2009).
CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC both cytoplasmic and membrane proteins. Plays a role in the quality
CC control of integral membrane proteins. {ECO:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; FM864216; CAT04999.1; -; Genomic_DNA.
DR AlphaFoldDB; C5J6A7; -.
DR SMR; C5J6A7; -.
DR MEROPS; M41.009; -.
DR EnsemblBacteria; CAT04999; CAT04999; MCJ_003080.
DR KEGG; mco:MCJ_003080; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OMA; DISDFRI; -.
DR Proteomes; UP000001491; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..754
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400358"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 31..186
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 208..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 713..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 500
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 754 AA; 83355 MW; C3845A03B0D832F4 CRC64;
MKQRMKKPSL GTFILILILI GILAYVLWQF LSPKLGYKSL SDLEQRIITN AKSATDDNFF
WAFGFDISDF RIKVVEQVGN RIESYQVVAD PTIIRLYQAG TGGVISENIL SQLGSSAPKV
NSWREIIQLA TKASLTSEII ENAINQKINN ALSLVGAGQS VSKNTIVNAN LPVIFNFDRP
RGNFLSSFIV PYIPFLLISL FGFWLFFRLS QNSQAGGGLF NPGKNQAIRI KSNKKFTDVA
GNAEVKEEIA EFVDYLKNPK KYAAAGAKIP KGILLGGPPG TGKTLLAKAT AGEANVPFFF
ISASNFVELY VGVGAKRVRE LFKEARAESP AIIFIDELDA IGRSRGSGIG GGHDEREQTL
NQLLVEMDGM VENSGILLIG ATNRTDVLDP ALLRPGRFDR SIIVGLPDIK EREEILKLHA
KGKRISQNIT LANIAKRTPG FSGAQLENVI NEATLLSVRE KTQVITGKQI DEAIDRVISG
PAKKNRVITE DERTMVAYHE AGHAVVGIKL RSGVKVQKIT IVPRGNTGGY NLMLPEHEKY
NSTKSELLAS IAAFMGGRAA EEIIYGKNEI STGAANDIEK ATKIARRMVT EFGMSNLGPI
QYEQDNSSPF LGRDYFKNAS FSSQVGHEID IEIREIISSS YKLAIATIQE HRLLLELIKD
TLLEKETIVF EEIQQLEQTL KPLPKSTEIE EKQKVNTKDI LEELMGSDFA NNQEKSYENE
DQNQNSLEAI NYNIDDQDDD KNDSESKIDS SKEQ
