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ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-)

 F0RZZ6_DESTD            Unreviewed;       626 AA.
F0RZZ6;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
25-OCT-2017, entry version 43.
RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
OrderedLocusNames=Dester_1039 {ECO:0000313|EMBL:ADY73677.1};
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
Desulfurobacterium.
NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73677.1, ECO:0000313|Proteomes:UP000007102};
[1] {ECO:0000313|Proteomes:UP000007102}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of Desulfurobacterium thermolithotrophum DSM
11699.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Acts as a processive, ATP-dependent zinc
metallopeptidase for both cytoplasmic and membrane proteins. Plays
a role in the quality control of integral membrane proteins.
{ECO:0000256|HAMAP-Rule:MF_01458}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01458};
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP-
Rule:MF_01458}.
-!- SIMILARITY: Belongs to the AAA ATPase family.
{ECO:0000256|RuleBase:RU003651}.
-!- SIMILARITY: In the C-terminal section; belongs to the peptidase
M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}.
-!- SIMILARITY: In the central section; belongs to the AAA ATPase
family. {ECO:0000256|HAMAP-Rule:MF_01458}.
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EMBL; CP002543; ADY73677.1; -; Genomic_DNA.
RefSeq; WP_013638629.1; NC_015185.1.
STRING; 868864.Dester_1039; -.
MEROPS; M41.001; -.
EnsemblBacteria; ADY73677; ADY73677; Dester_1039.
KEGG; dte:Dester_1039; -.
eggNOG; ENOG4105C3H; Bacteria.
eggNOG; COG0465; LUCA.
KO; K03798; -.
OMA; MNKRWRN; -.
OrthoDB; POG091H02HH; -.
Proteomes; UP000007102; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
HAMAP; MF_01458; FtsH; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR005936; FtsH.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011546; Pept_M41_FtsH_extracell.
InterPro; IPR000642; Peptidase_M41.
InterPro; IPR037219; Peptidase_M41-like.
Pfam; PF00004; AAA; 1.
Pfam; PF06480; FtsH_ext; 1.
Pfam; PF01434; Peptidase_M41; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF140990; SSF140990; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01241; FtsH_fam; 1.
PROSITE; PS00674; AAA; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
ECO:0000256|RuleBase:RU003651};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000007102};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
ECO:0000313|EMBL:ADY73677.1};
Membrane {ECO:0000256|HAMAP-Rule:MF_01458};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01458,
ECO:0000313|EMBL:ADY73677.1};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
ECO:0000256|RuleBase:RU003651};
Protease {ECO:0000256|HAMAP-Rule:MF_01458,
ECO:0000313|EMBL:ADY73677.1};
Reference proteome {ECO:0000313|Proteomes:UP000007102};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
TRANSMEM 12 28 Helical. {ECO:0000256|HAMAP-
Rule:MF_01458}.
TRANSMEM 104 123 Helical. {ECO:0000256|HAMAP-
Rule:MF_01458}.
DOMAIN 189 328 AAA. {ECO:0000259|SMART:SM00382}.
NP_BIND 197 204 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
COILED 551 578 {ECO:0000256|SAM:Coils}.
ACT_SITE 420 420 {ECO:0000256|HAMAP-Rule:MF_01458}.
METAL 419 419 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01458}.
METAL 423 423 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01458}.
METAL 495 495 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01458}.
SEQUENCE 626 AA; 69526 MW; 876F842A9D118074 CRC64;
MDKLKEIGKS LALWLTIALL IILAFNFFNS EQLKKHTEPF STFLQQVEKG EVKKVVIQGQ
KVTGVTKDNK PFETYLPPGY TSVIDKLAEK NVEIQVKPEE GSPWYITVLV SWLPMIFLIL
LWISMMRQMS MGSNKALSFA KSRAKVFIDN KPKVTFKDVA GIDEVKEEVS EIVDFLKNPK
KFQQLGGRIP KGVLLAGAPG TGKTLLAKAI AGEANVPFLS VSGSEFVEMF VGVGASRVRD
LFEQAKRHAP CIVFIDEIDA VGRKRGAGFT GGHDEREQTL NQLLVEMDGF ESSEGIIVIA
ATNRPDILDP ALLRPGRFDR QIHVPLPDVR GRLEILKIHT KDKPLAEDVD LEVIARSTPG
FSGADLANIV NEAALIAARK NHGKITMEDF EEAKDKVTMG IERKSMVLSE EEKVTTAYHE
AGHTLIAKLL PNADKVHKVT IIPRGKALGI TQQLPEEDRY TYTKDYLLDR LCVLFGGRVA
EELALGTIST GAGNDIERAT EIAKKMVAEW GMSDTIGPIA VKIREQFGEP AELISEEMKK
LIDKEVRKII QETYERTKEL ISQNMDKLEN LAKALLERET LTGEEIDMAM KGELKSNDMD
STNPPAGSKK ERKEEIPPSL NPQLEA


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