FTSH_LEPBD
ID FTSH_LEPBD Reviewed; 768 AA.
AC C7N914;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Lebu_0737;
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX NCBI_TaxID=523794;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-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; CP001685; ACV38645.1; -; Genomic_DNA.
DR RefSeq; WP_015768993.1; NC_013192.1.
DR AlphaFoldDB; C7N914; -.
DR SMR; C7N914; -.
DR STRING; 523794.Lebu_0737; -.
DR EnsemblBacteria; ACV38645; ACV38645; Lebu_0737.
DR KEGG; lba:Lebu_0737; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000001910; 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 Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..768
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400349"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 55..139
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 161..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 647..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..745
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 768 AA; 85367 MW; BB9C939EBCD18FB8 CRC64;
MADRDKNDIR KRLEELRKDN NRRNNRQDNG NRSPFSGFLF FIFVILLFTF TLLFHRDIQT
YFQEKREISY TEFVSKTQKG DFSEINEKDD KLISQVKENG KDVLYYTKKI TDRVGDEPNI
ISAIGQKKVK LNSLQPSGGG FFLLLLGQFL PMIIMIGLMV YLAKKMVGGS QGGGPGNIFG
FGKSRVNKID KKPDVKFDDV AGVDGAKEEL REVVDFLKNP EKYTKAGARV PKGVLLLGRP
GTGKTLLAKA VAGESGASFF SISGSEFVEM FVGVGASRVR DLFEKAKESS PSIIFIDEID
AIGRRRSVGK NSGSNDEREQ TLNQLLVEMD GFETDTKVIV LAATNREDVL DPALLRAGRF
DRRVTVDAPD LQGRIAILKV HSRNKKLARD VKLEDIAKIT PGFVGADLAN LLNEAAILAA
RRASDTIKMA DLDEAVDKIG MGLGQKGKII KPEEKKLLAY HEAGHAIMTE LTPGADPVHK
VTIIPRGDAG GFMMPLPEEK LVTTSRQMLA EIKVLFGGRA AEEIGLEDVS TGAYSDIKRA
TKVARAYVES VGMSKKLGPI NFENSDDEYS FTPNKSDETV REIDLEIRKI LTEEYFNTLN
TLQDNWEKLE QVVELLLKKE TITGDEVRRI IAGEKAEDIL KGTEVKEESI QKGSEGIVQT
SENSIEESQE NKTVEAEVHD SNLKSDTEKL AEAVREITGE TGGVLEPTEK NDFDKDSDDN
EKNDDDNENS DDSSKNDSDS DDENENSDNK SEKNKKRKSN FKLPSFME
