FTSH_PARD8
ID FTSH_PARD8 Reviewed; 684 AA.
AC A6LD25;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BDI_1854;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43589.1; -; Genomic_DNA.
DR RefSeq; WP_005854893.1; NC_009615.1.
DR AlphaFoldDB; A6LD25; -.
DR SMR; A6LD25; -.
DR STRING; 435591.BDI_1854; -.
DR MEROPS; M41.A17; -.
DR EnsemblBacteria; ABR43589; ABR43589; BDI_1854.
DR KEGG; pdi:BDI_1854; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_10; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR BioCyc; PDIS435591:G1G5A-1906-MON; -.
DR Proteomes; UP000000566; 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; IPR018247; EF_Hand_1_Ca_BS.
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..684
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400367"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 43..138
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 160..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 647..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 684 AA; 76090 MW; C58AA2FB81486CFB CRC64;
MENKNDMFNK TPKSGKPKMF RFNLYWMYGL IFIMLVALYM TNDSSGTKEL GWTEFQKLAQ
ENVFDKMTVY NKKNLVEATV KNGKTEQVFG NMDVSKIGVS PKVYVKIPSA DKFSDFYDKA
VADSHIDTQV RFEEGDDAIW NFLVSFGPII LLIGVWMFLM RRMSGGTGAG PGGVFSVGKA
KAQLFDKDND RKVTFKDVAG LAEAKQEVEE IVSFLKNPEK YTELGGKIPK GALLVGPPGT
GKTLLAKAVA GEANVPFFSL SGSDFVEMFV GVGASRVRDL FRQAKEKSPC IVFIDEIDAV
GRARGKNANM NSNDERENTL NQLLTEMDGF GSNSGVIILA ATNRADILDK ALLRAGRFDR
QIHVELPDLN ERKEIFGVHL RPIKIDESVD AEFLARQTPG FSGADIANVC NEAALIAARN
GKKFVQKEDF MNAVDRIVGG LEKRSKITTE EERKCIANHE AGHATLSWLL EHANPLVKVT
IVPRGKALGA AWYLPEERQI TTREQLQDEM CATLGGRAAE ELVLGKISTG ASNDLERVTK
QAYAMVVYFG MSDKLPNLNY YDSTGQDWGF TKPYSEETAK LIDTEVQKII NEQYDRAKRI
LSENKEGHSK LAQVLLDREV IYSEDVEHIF GKRAWISRSQ EILELQEKAN GKNKENADKE
AEADATTENV TDTPTEENKT GKIA
