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Database: UniProt
Entry: B7R0L5_9EURY
LinkDB: B7R0L5_9EURY
Original site: B7R0L5_9EURY 
ID   B7R0L5_9EURY            Unreviewed;       401 AA.
AC   B7R0L5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Cell division protein FtsH {ECO:0000313|EMBL:EEB74570.1};
GN   ORFNames=TAM4_515 {ECO:0000313|EMBL:EEB74570.1};
OS   Thermococcus sp. AM4.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74570.1, ECO:0000313|Proteomes:UP000009277};
RN   [1] {ECO:0000313|EMBL:EEB74570.1, ECO:0000313|Proteomes:UP000009277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM4 {ECO:0000313|EMBL:EEB74570.1,
RC   ECO:0000313|Proteomes:UP000009277};
RX   PubMed=22123768; DOI=10.1128/JB.06259-11;
RA   Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H.,
RA   Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
RT   "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT   sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense
RT   of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide.";
RL   J. Bacteriol. 193:7019-7020(2011).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; CP002952; EEB74570.1; -; Genomic_DNA.
DR   RefSeq; WP_014121457.1; NC_016051.1.
DR   AlphaFoldDB; B7R0L5; -.
DR   STRING; 246969.TAM4_515; -.
DR   GeneID; 7418508; -.
DR   KEGG; tha:TAM4_515; -.
DR   eggNOG; arCOG01307; Archaea.
DR   HOGENOM; CLU_000688_21_2_2; -.
DR   OrthoDB; 77269at2157; -.
DR   Proteomes; UP000009277; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF83; VESICLE-FUSING ATPASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW   Cell cycle {ECO:0000313|EMBL:EEB74570.1};
KW   Cell division {ECO:0000313|EMBL:EEB74570.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003651}.
FT   DOMAIN          151..288
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          78..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  45480 MW;  01F95C01C37D355D CRC64;
     MPVDLSGPLL SAFRKAKREF EDAIKKGDKE TARKKALECA RILKQLSKYD EFNCESYLKK
     AKKWEVIAKE VEEGRYGAKR KHKPVKEGGK GGKGGSEASV DEEDQFKRYV ENLIARSKVK
     WSDIGGLDEV KRLIMETVVI SALQRPQSIQ PWKGILLFGP PGTGKTLLAS AAAGSLNATF
     FSVKASNVLS KYFGESTKII SALYEVARER APSIVFMDEI DALTTKRSGD QSEASRRMLS
     TLLTELDGFQ DKGSDVLVLT LAATNTPWDL DEAVLSRFPR RIYVPLPDKK ATKEIIKINT
     RGLDISRLDL DAIAEESVRR LYSGRDIKNL CQEAVWNMIR EENPDLHKLA ELPYEKLRRR
     SLRTRPLEMR DFEAAFKKIK SPLTRKDIER YEKWAEEFGG W
//
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