FTSH_SYNC1
ID FTSH_SYNC1 Reviewed; 646 AA.
AC Q3A579;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Pcar_1229;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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; CP000142; ABA88478.1; -; Genomic_DNA.
DR RefSeq; WP_011340952.1; NC_007498.2.
DR AlphaFoldDB; Q3A579; -.
DR SMR; Q3A579; -.
DR STRING; 338963.Pcar_1229; -.
DR EnsemblBacteria; ABA88478; ABA88478; Pcar_1229.
DR KEGG; pca:Pcar_1229; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_7; -.
DR OMA; RRSNGMP; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000002534; 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..646
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400368"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 26..120
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 142..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 438
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 646 AA; 71684 MW; 9009F626DA68D4FC CRC64;
MTRSLLWQMV IVLGAILMVN YVLTTLTPQT QEPVVDVSYS RFKTELAADN VAAITFEGNN
VVGNLRERTI LNRVEGTEEV QSFLRFRTTM PPVTDTRLLD DLEQRKVDVK VRPESKPSPW
ATAMIYMLPW LLIVGVWWFV IKGMRTRQGP GGGMMGGFSK SGAKMYTKER SRVTFADVAG
LDEAKQELME IIEFLRNPKK FMRLGAKAPR GVLLVGPPGT GKTLMARAVA GEAEVPFFTI
SASQFIEMFV GVGASRVRDL FNNAKKNAPS IIFIDELDAV GRSRGTGLGG GNDEREQTLN
QLLSEMDGFE AHDEVIVMSA TNRPDVLDPA LLRPGRFDRQ VTVERPDWRA REEILKVHTR
QVPIDEDVDL QIIARSTPGM CGADLENLVN EAALIAAREN AQKVTMQHFE QAKDRVLMGT
ERKLVMSQQE KRITAYHEAG HTLLARLSPG ADPIHKVSII PRGQALGVTQ QLPVDDRYHY
SRSYLMTRIA VSLGGRAAEK AIFEEYSTGA QNDLKQATDL AEKMVCQWGM SERVGPMSIN
RGEEHPFLGR KLASDNAFSQ HMAWIIDQEI EKVVKAGEQA ADEIIANHLP VLKKLADALL
EEEVLDRTRV DEVLRETGIE VQDDPAAHPD GDHVLQGELA GGAVEG
