ID A0A0D8IF20_9CLOT Unreviewed; 591 AA.
AC A0A0D8IF20;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN Name=ftsH3 {ECO:0000313|EMBL:AKL94886.1};
GN Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN ORFNames=CACET_c14220 {ECO:0000313|EMBL:AKL94886.1}, TZ02_04215
GN {ECO:0000313|EMBL:KJF27811.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL94886.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL94886.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL94886.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF27811.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF27811.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) 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:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR EMBL; CP009687; AKL94886.1; -; Genomic_DNA.
DR EMBL; JYHU01000004; KJF27811.1; -; Genomic_DNA.
DR RefSeq; WP_044823661.1; NZ_JYHU01000004.1.
DR AlphaFoldDB; A0A0D8IF20; -.
DR STRING; 84022.CACET_c14220; -.
DR KEGG; cace:CACET_c14220; -.
DR PATRIC; fig|84022.5.peg.2882; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
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 CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651}; Cell cycle {ECO:0000313|EMBL:KJF27811.1};
KW Cell division {ECO:0000313|EMBL:KJF27811.1};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01458};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Reference proteome {ECO:0000313|Proteomes:UP000035704};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 188..327
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 591 AA; 65779 MW; 091C6FF9579387D8 CRC64;
MKKISKKKLM LAIGMFVVIL SIISFGIYRQ YFYSENPIEV SYGEFLEKIE ENQINKVFLM
DSPKIKGELK DGQEFITDHP RTDNLKEMLL TADVIVVEVG EQHSVVQVIT FIIVIGALAG
MAFILSKQGS KQASKEYDKM SSVEFSTQKE STITFANIAG NEEAKENVME LVDFLKNPQK
YQRYGARMPK GVILYGPPGT GKTLMAKALA SEAGVDFLAV SGSDFVQVYA GLGAGRIRNL
FKNAREKGKC VIFIDEIDAI GKKRDRGGLG GSDESDRTLN ALLTEMSGFK GSEGIIIMAA
TNRLDILDEA LLRPGRFDRQ IEVGLPDLKA RQDILKLYTQ NRPIATTISI ERIAQQTVYF
SGAKLENLMN EAAIYAAREN ASFISEKHVD KAFYTVVAGE EKKDRSNIKE SERRITAYHE
AGHTIATKLL CPENKVTKVT IIPSTKGAGG FSMNIPPDSM YHKKKDMFHS IKIALAGRAV
EEIIFGEENI TTGASNDIQK ATEILVAMIK QFGMNDEVGM INYDILLGQP GGVDQRLAEI
CNKEMKRLYE ETKVLIEKNI HLVHAVTEEL MARETLKEEE INKIIENNKV A
//
