ID   A0A2M8P168_9CHLR        Unreviewed;       633 AA.
AC   A0A2M8P168;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   31-JUL-2019, entry version 8.
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   Chloroflexi bacterium.
OC   Bacteria; Chloroflexi.
OX   NCBI_TaxID=2026724 {ECO:0000313|EMBL:PJF31297.1};
RN   [1] {ECO:0000313|EMBL:PJF31297.1}
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
RT   Horizontal Gene Transfer.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc
CC       metallopeptidase for both cytoplasmic and membrane proteins. Plays
CC       a role in the quality control of integral membrane proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       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
CC       M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PJF31297.1}.
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DR   EMBL; PGTK01000004; PJF31297.1; -; Genomic_DNA.
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:ATPase activity; IEA:UniProtKB-UniRule.
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   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};
KW   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|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|HAMAP-Rule:MF_01458};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {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       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      179    318       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     187    194       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   REGION      592    633       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      554    581       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    596    623       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    410    410       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       409    409       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       413    413       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       489    489       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                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
//