ID K8ELQ1_9FIRM Unreviewed; 493 AA.
AC K8ELQ1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000313|EMBL:CCO09391.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:CCO09391.1};
GN Name=ftsH {ECO:0000313|EMBL:CCO09391.1};
GN ORFNames=DESHY_80058 {ECO:0000313|EMBL:CCO09391.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO09391.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO09391.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCO09391.1}.
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DR EMBL; CAOS01000015; CCO09391.1; -; Genomic_DNA.
DR RefSeq; WP_008413393.1; NZ_FQXF01000011.1.
DR AlphaFoldDB; K8ELQ1; -.
DR STRING; 1121428.DESHY_80058; -.
DR eggNOG; COG0465; Bacteria.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000009315; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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; IPR027417; P-loop_NTPase.
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; 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|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCO09391.1};
KW Metalloprotease {ECO:0000313|EMBL:CCO09391.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CCO09391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315}.
FT DOMAIN 98..243
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 493 AA; 53845 MW; 41900A43AF2B408C CRC64;
MLKEISIGLA AALLVFAAVA GYDITPVIFL LAFGGALLYL TGAKGMVKSG FGQAATPARR
QDISFDDIGG QAVAIKELKE ALDFIINHQA IQSLGIRPLK GILMTGPPGT GKTLMARAAA
GYTDAVFVSA SGSDFVEMYA GVGAQRVRKL FQTARATAVK QKKKNAIIFI DEIEVLAAKR
GQHAGHMEYD QTLNALLVEM DGIKADDNVR LLIMAATNRV DMMDPALLRP GRFDRQVKVD
LPDKAGRLEI LKLHTRNKPL ADDVDLSRIA KETFGFSGAH LESLANEAAI LAMREGLKEI
HYRHFHEAVD KVIMGEKLDR QPNPDELKRV AVHEIGHAFI SEWVRPGSVS TLTVTPRGGA
LGYMRQNPED DTYLYTKDYL ENQIAIMLAG AVAEEIVYGN RSTGAANDYE KALQTADTMI
KAGMSKLGVV SLESLPGELK HQVVSEIING QEQRVYRVMQ QHQDFLQATV QVLLEQEKIS
GEEFRALIPP LAA
//
