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Database: UniProt
Entry: W6SCV9_9CLOT
LinkDB: W6SCV9_9CLOT
Original site: W6SCV9_9CLOT 
ID   W6SCV9_9CLOT            Unreviewed;       580 AA.
AC   W6SCV9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=ftsH1 {ECO:0000313|EMBL:CDM67425.1};
GN   Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   ORFNames=CM240_0255 {ECO:0000313|EMBL:CDM67425.1};
OS   Clostridium bornimense.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM67425.1, ECO:0000313|Proteomes:UP000019426};
RN   [1] {ECO:0000313|EMBL:CDM67425.1, ECO:0000313|Proteomes:UP000019426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Complete genome sequence of Clostridum sp. M2/40.";
RL   Submitted (NOV-2013) 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; HG917868; CDM67425.1; -; Genomic_DNA.
DR   RefSeq; WP_044035882.1; NZ_HG917868.1.
DR   AlphaFoldDB; W6SCV9; -.
DR   STRING; 1216932.CM240_0255; -.
DR   KEGG; clt:CM240_0255; -.
DR   PATRIC; fig|1216932.3.peg.236; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_9; -.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000019426; Chromosome 1.
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 YME1L1; 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};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019426};
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          182..322
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          532..567
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        414
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         190..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         491
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   580 AA;  63691 MW;  4AA2408721F90053 CRC64;
     MNKIKKNYIL IPIFTAILSL IFMIIIASNT TTSINKSYSN FTEDLNSHNI STVIMDTSPN
     MTVILNNGEK YSTDNPKTDN LKETLLLNNI KVKDETVAPL IKTLPSGIFV VSLLTIMFML
     IAKARGGSGS MTSMDMEDFS KNKKVALDFN SVAGNDEAKE SLMDIVDFLK SPEKYQKYGA
     RMPKGVILYG SPGTGKTLLA KAVAGEAGVP FYALSGSDFV QVYVGVGAAR IRNLFKKAKS
     HGKAVIFIDE IDAIGKKRGN SKGGGNNDER DQTLNALLTE MSGFGQEEGI VVIAATNRLD
     MLDDALLRPG RFDRHIEVSL PDVNAREKIL SLHLKNKPHD NLDIKDIAKK TVYFSGAKLE
     SLVNESAILA AKDDSDTITN KHIEAAYSIT LAGYDKKETS YLSKEDKLLT SYHEAGHGLV
     SMLLLPKDKV SKITIIPTTK GAGGYTLTIP EDKNYHKMNY LKNKIKVLLG GRAAEEIIFG
     KENISTGAEN DISQTTDIAL KMISEYGMGD TLGLIKLSSV GSLYGSYGNP VIEECKKLLD
     NLYEETLELL RENKNKLDSL ALELLEKETL YDTELEKFVS
//
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