FTSH_SYNFM
ID FTSH_SYNFM Reviewed; 647 AA.
AC A0LN68;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Sfum_3197;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
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; CP000478; ABK18870.1; -; Genomic_DNA.
DR RefSeq; WP_011699995.1; NC_008554.1.
DR AlphaFoldDB; A0LN68; -.
DR SMR; A0LN68; -.
DR STRING; 335543.Sfum_3197; -.
DR MEROPS; M41.021; -.
DR PRIDE; A0LN68; -.
DR EnsemblBacteria; ABK18870; ABK18870; Sfum_3197.
DR KEGG; sfu:Sfum_3197; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_7; -.
DR OMA; QRTYAPR; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000001784; 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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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..647
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400405"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 61..134
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 156..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 647 AA; 72010 MW; F5A1E418DAF50D5B CRC64;
MARKSDEDTN PMDKFMDRLR GSPGDGGPGR PDPSQRKVHF SIWYFILALL LIVWMQTYMG
EQQSEKISYS EFKQRVHDGN VQNLVIEHDR ITGTMKENDG PGRRFNTIRV EDPELVKQLE
AKNIRFSGDV QNPWLGLITW WLLPFAIMIF FWSFLMRRMG GGPQGVLSVG KARVKIFAEK
EITITFDDVA GIDEAKGELE EIVQFLKDPG KFQRLGGRIP KGVLLVGAPG TGKTLLAKAV
AGEAGVPFFS MSGSEFVEMF VGVGAARVRD LFGQAKDHAP CIIFIDELDA LGKARGLNPI
GGHDEREQTL NQLLVEMDGF DPRSGVIIMA ATNRPEILDP ALLRPGRFDR HVAIDKPDIR
GREAILRVHV KEVKLGSEVD LKKIAGMTPG FVGADLANLV NEAALVAARR DRDEVTMADF
QEAADRIIGG LEKKNRAMNP KEKEIVAYHE AGHALVAMLL PNVDPVNKVS IIPRGIAALG
YTQQLPTEDR YLMTRNELLD RLQVLLGGRV SEEIIFGDVS TGAQNDLQRA TDIARSMVME
YGMSERLGPL TYTRDPRSAH LDLGLGSRER DYSEMIAQEI DEEITRIVED AHEKVRATLK
RERGCLEKLA KILLEKESID GEELKQFCQE VKSHIARDPV QVEGGAA
