FTSH_PELPD
ID FTSH_PELPD Reviewed; 623 AA.
AC A1AT11;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Ppro_2884;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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 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; CP000482; ABL00482.1; -; Genomic_DNA.
DR RefSeq; WP_011736717.1; NC_008609.1.
DR AlphaFoldDB; A1AT11; -.
DR SMR; A1AT11; -.
DR STRING; 338966.Ppro_2884; -.
DR EnsemblBacteria; ABL00482; ABL00482; Ppro_2884.
DR KEGG; ppd:Ppro_2884; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_7; -.
DR OMA; RRSNGMP; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000006732; 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..623
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_5000182149"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 29..117
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 139..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 623 AA; 68435 MW; 5ABA905BB915D640 CRC64;
MNQSFWRPLF AILLFMLVFH LTNIFFAQQG AQVAQISYSR LRAELAQDNI KKITLKGTAV
TGEFRGKTRV SALVQGKEQQ REFTGFSSVL PTIDDQTLVP ELMARKVEVS ALSTETPLLL
NALIYVAPWV ILIAIWWVGM RSMRSQGPSG MMGGFSRSGA KAYLAGDKMA VSFKDVAGME
DSKQELKEVV DYLRNPKQFA RIGGKVPKGV LLVGPPGTGK TLLARAVAGE AGVAFFSISA
SQFIEMFVGV GASRVRDLFT NAKKAAPSIV FIDELDAVGR SRGAGFGGGH DEREQTLNQL
LSEMDGFDQH EEVIVLAATN RPDVLDPALL RPGRFDRHVV IERPDWRDRE KILQVHVRKI
TMNGRIDLGV IARGTPGMTG ADLESLVNEA AILASRENAA AVTMEHLEKA KDKILMGSER
RMIISLEEKR ITAYHEAGHT LVARLLPGTD PIHKVTIIPH GMALGVTQQL PEDDRYHYPQ
SYLENRLVVA MGGRVAERLA FGEVSSGAQG DLKQVTSLAE KMVCQWGMSE KVGGMTFSRG
EEHPFLGMKL AEEKTFSEAM AWRIDQEIAA FITRAEQRAG DLLSANRERL DLLAQALQDE
ETLDGSRVDE IIGSLNTAQA PPP
