FTSH2_PHYMT
ID FTSH2_PHYMT Reviewed; 686 AA.
AC B3QZS3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 2 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH2 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=ATP_00273;
OS Phytoplasma mali (strain AT).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX NCBI_TaxID=482235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT;
RX PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA Reinhardt R., Seemueller E.;
RT "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT Phytoplasma mali'.";
RL BMC Genomics 9:306-306(2008).
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; CU469464; CAP18460.1; -; Genomic_DNA.
DR AlphaFoldDB; B3QZS3; -.
DR SMR; B3QZS3; -.
DR STRING; 37692.ATP_00273; -.
DR MEROPS; M41.009; -.
DR EnsemblBacteria; CAP18460; CAP18460; ATP_00273.
DR KEGG; pml:ATP_00273; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OMA; HADPLNK; -.
DR Proteomes; UP000002020; 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..686
FT /note="ATP-dependent zinc metalloprotease FtsH 2"
FT /id="PRO_0000400376"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 33..178
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 200..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 494
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 272..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 686 AA; 78477 MW; 020B0EE244E2BDFA CRC64;
MKKNIKDIFK NFNIFWFCFI FLLLSLLYCL IMMEISHQHD NNKPSEIIAV LKEIKELQTK
STEESKKESK ESKESKEDKT KIIKIKKFDI HETSNYGSYL IVFQWGTGNK DSFEWEKELK
FPNVDQETYK EIMKICFEII GTPIDKKDNI TNLSQMITKI KEKTNLIPLQ RIPYQPYFGF
APFISAVNIC ILIIIFYFIY NSIEKTSAQI SGKNLNISRQ KVLVNQQEFT FKDIAGADEE
KEEMSELINF LKNPFKYEAM GARIPKGVLL YGPPGVGKTL LAKAVAGEAK VPFFAVSGSD
FIEVYVGLGA SRIRKLFNEA KQNAPCIIFI DEIETISHQR GSVNYSNSEH DQTLNQLLVE
MDGFTKNIGV IVMAATNQPE SLDLAVTRPG RFDRHFHITL PSVKDREAIL KLHARNKKFN
DDVDFESLAK QTPGFNGAQL EAILNESALL ATRRNVLVIC NEDISEALDR VLMGPSKKSK
KYNDKEKRMV AYHESGHAVI GLKLPEADQI QKVTIIPRGN AGGYNLTLPQ EETFFSSKKR
LLAQITSFLG GRAAEEVVFQ DVSNGAYSDF KYATEIAKKM VTQYGMSDLG PIQYMENNFY
KNFSDSKAVE IDKEIQKIID YCYQNAKKII TENRDLLDLI SKYLLEIETI TQKDLEEILN
TGIIEWWEKD KLKKNLQKSE KEDCNK
