ID   FTSH2_METI4             Reviewed;         641 AA.
AC   B3DY14;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Minf_1912;
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum.
OX   NCBI_TaxID=481448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4;
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; 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; CP000975; ACD83966.1; -; Genomic_DNA.
DR   RefSeq; WP_012464248.1; NC_010794.1.
DR   AlphaFoldDB; B3DY14; -.
DR   SMR; B3DY14; -.
DR   STRING; 481448.Minf_1912; -.
DR   EnsemblBacteria; ACD83966; ACD83966; Minf_1912.
DR   KEGG; min:Minf_1912; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_0_0; -.
DR   OMA; QYGMTER; -.
DR   OrthoDB; 190468at2; -.
DR   Proteomes; UP000009149; 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 inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..641
FT                   /note="ATP-dependent zinc metalloprotease FtsH 2"
FT                   /id="PRO_0000400354"
FT   TOPO_DOM        1..100
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        122..641
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          593..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         193..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         415
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         491
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   641 AA;  70258 MW;  4241452D4FF8E2D1 CRC64;
     MLAYYVSVNQ GPGIEQKSLP QLTRLLDQGR VKALVFIRDT STGQTFLEGR YTRPAGPTEN
     AEIVVPFRTV VDLEFNRDLK QFLASKGFPE IDVKVIHNFW GQAFLSVLPF LLFILALYFL
     FRQQIRMAGR GAFSFGKSRA RLLSGGKTKV TFKDVAGVEE AKEEVQELVE FLKDPKKFQK
     LGGRIPKGVL MVGPPGTGKT LLAKAIAGEA DVPFFSISGS DFVEMFVGVG ASRVRDMFEQ
     ARRHAPCIVF IDEIDAVGRA RGTGLGGGHD EREQTLNALL VEMDGIESQE GVIVIAATNR
     KDVLDPALLR PGRFDREVRV NLPDIRGREQ ILRVHAQKIK LSKNADLSAL ARGTPGFSGA
     ELANLINEAA LIAAKKGKDN VDQPDLEEAR DKVRWGKERR SLAMSEEERK TTAYHEAGHA
     VLNVLLENTD PIHKVTIIPR GPALGVTMML PASDKYNARK KEVLDDLCVA MGGRVAEEVF
     LGDISSGASG DIRQATWYAR KMVCEWGMSE KLGMVHYADD SSMVFLGREL GTSRGYSEAT
     ARAIDHEVQH FIQAAYEKAK RIILEHKDKV EALAQALLEY ETLNADQVTE IVKTGKMTNP
     PSKNSSPVSN GGEASSTKSP ARQEETTKDG GLLPGLEGAP A