FTSH3_CONWI
ID FTSH3_CONWI Reviewed; 749 AA.
AC D3EZK2;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 3 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH3 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=Cwoe_5435;
OS Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS 100937 / ID131577).
OC Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC Conexibacteraceae; Conexibacter.
OX NCBI_TaxID=469383;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Conexibacter woesei DSM 14684.";
RL Submitted (JAN-2010) 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: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; CP001854; ADB53840.1; -; Genomic_DNA.
DR RefSeq; WP_012936891.1; NC_013739.1.
DR AlphaFoldDB; D3EZK2; -.
DR SMR; D3EZK2; -.
DR STRING; 469383.Cwoe_5435; -.
DR EnsemblBacteria; ADB53840; ADB53840; Cwoe_5435.
DR KEGG; cwo:Cwoe_5435; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_11; -.
DR OMA; YDKQGGG; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000008229; 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..749
FT /note="ATP-dependent zinc metalloprotease FtsH 3"
FT /id="PRO_0000400339"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 97..186
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 208..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 505
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 749 AA; 79931 MW; 3B188A0D57009E77 CRC64;
MTGDPPERRS NGDRLPAERP PSNEGQTPPR KPGRNEPGSP PDWRVTPAPD GRGTPRRGRN
GGGMRPFRFP GGRWGILVFI LVLLGLNWWI SSNALAPSER VRVPYSPNFI QQVRDGNVKE
ISSTGASIQG DFRADVTYPP KDDKDSVTAK KFSTEVPAFA DTDELSKLLQ DNDVTVNASP
ADNGPSLLVS ILLGFGPVIL IIALFVFLSR RMAGAAGGGM MSFGRSRARR SEGGEAQVTF
RDVAGIDEAE AELNEIVDFL KNPQKYQRLG GKIPKGVLLS GQPGTGKTLL ARAVAGEAGV
PFFSMSASEF VEMIVGVGAS RVRDLFRQAK EAAPAIIFID ELDAIGRARG GGRGSFGGND
EREQTLNQIL TEMDGFEPTT AVIVIAATNR PEILDAALLR PGRFDRRVTV AAPDRNGRLM
ILKVHTRSVP LADDVDLESI ASSTPGMVGA DLANLVNEAA LLAARRGHVK VTNSDVADAL
EKVVLGAERK VMMSDDDRRR TAYHESGHAI VGMLTAGADP VRKVSIIPRG QALGVTFSSP
DADKYNYDER YLVGKIKVAL GGRVAEEIVF GDLTTGAESD IQQLTGIARQ MVGRWGMSRA
IGPIAVLPSE GNGPLLPGVA ETSESTQRLV DEEVRRIVDS AHAEVTRLLR EHRANLDSLV
AGLLDQETLD EADAYEAAGL EHMRPERVEP PAPRPSRRDG GRSVAAGPVP HGLEAPERPA
QIAAPGADEP EPPTNGSGEL GGSVRAGDA
