ID   A0A2M8P168_9CHLR        Unreviewed;       633 AA.
AC   A0A2M8P168;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   19-JAN-2022, entry version 14.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN   Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   ORFNames=CUN51_04735 {ECO:0000313|EMBL:PJF31297.1};
OS   Candidatus Thermofonsia Clade 1 bacterium.
OC   Bacteria; Chloroflexi; Candidatus Thermofonsia;
OC   Candidatus Thermofonsia Clade 1.
OX   NCBI_TaxID=2364210 {ECO:0000313|EMBL:PJF31297.1, ECO:0000313|Proteomes:UP000228921};
RN   [1] {ECO:0000313|EMBL:PJF31297.1, ECO:0000313|Proteomes:UP000228921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP2_2F {ECO:0000313|EMBL:PJF31297.1};
RA   Ward L.M., Hemp J., Shih P.M., Mcglynn S.E., Fischer W.;
RT   "Evolution of Phototrophy in the Chloroflexi Phylum Driven by Horizontal
RT   Gene Transfer.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJF31297.1}.
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DR   EMBL; PGTK01000004; PJF31297.1; -; Genomic_DNA.
DR   Proteomes; UP000228921; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651}; Cell cycle {ECO:0000313|EMBL:PJF31297.1};
KW   Cell division {ECO:0000313|EMBL:PJF31297.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_01458};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   TRANSMEM        95..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          179..318
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         187..194
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   REGION          592..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          554..581
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        596..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           409
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           413
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           489
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   633 AA;  69082 MW;  B7CD27E724A351CD CRC64;
     MAIFLGVRGG GSSGSELKLS ELAQQIISGT PRISAIAVAQ NEVRVTYAGS SRPPAITRKD
     PSMPLPEQLI SLGVPKELVA QLPIEYVQPN DITPFFSILV SLLPIILIAG FFFLMLRQAQ
     GSNNQAISFG KSRARMFTGD RPTVTFDDVA GADEAKEELR EVVEFLKEPD KFVQLGARIP
     KGVLLIGSPG TGKTLLAKAV AGEAGVPFFS ISGSEFVEMF VGVGASRVRD LFDQAKRHSP
     CIIFIDEIDA VGRHRGAGLG GSHDEREQTL NQILVEMDGF DTDTNVIVIA ATNRPDILDP
     ALMRPGRFDR RVVLDRPDVK GREAILRVHS RGKPLAADVD LAVLSRTTPG FVGADLENLM
     NEAAILAARK NKKTISMRDC EEAIYRVVLG PERKSRVISE EQKRLVAYHE AGHAIVGHFL
     PNCDPIRKIT IVPRGISGGS VLSVPEDDMG PETRARIEDA IAQALGGRAA EAIVFGEVTT
     GAGGGNGSDL ATVTRYARAM VTRFGMSDRL GPMIFGQKEE MVFLGREIAE QRDYSEAIAE
     IIDEEVKKIV DEAYQRALAV LTEHREELER VAQRLMEVET IDYEEFMQLM GESPATNRRK
     RPEMLPKPAE KPATQREQRD DLPPRMGTAA SPA
//