ID Q5UYS9_HALMA Unreviewed; 492 AA.
AC Q5UYS9;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cell division protein FtsH {ECO:0000313|EMBL:AAV47573.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:AAV47573.1};
GN Name=ftsH {ECO:0000313|EMBL:AAV47573.1};
GN OrderedLocusNames=rrnAC2818 {ECO:0000313|EMBL:AAV47573.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV47573.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV47573.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809
RC {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; AY596297; AAV47573.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5UYS9; -.
DR STRING; 272569.rrnAC2818; -.
DR PaxDb; 272569-rrnAC2818; -.
DR EnsemblBacteria; AAV47573; AAV47573; rrnAC2818.
DR KEGG; hma:rrnAC2818; -.
DR PATRIC; fig|272569.17.peg.3392; -.
DR eggNOG; arCOG04368; Archaea.
DR HOGENOM; CLU_646568_0_0_2; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0000502; C:proteasome complex; 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 CDD; cd19481; RecA-like_protease; 1.
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; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF114; AAA DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:AAV47573.1};
KW Cell division {ECO:0000313|EMBL:AAV47573.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:AAV47573.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
FT DOMAIN 251..386
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 492 AA; 54963 MW; 44E5ADF2B4E090FC CRC64;
MRLRYTASNV LPVAMFETHR GGILPWCRPS GLRVTYTGCV VTSVGMSNPE LDVVEFLLTA
TIYSERRDLE PDDLPASYRS VFWSDGEIER PLSVTNSTAS EATGVERPWA AISGLMFTDR
DDFSGSISMT DRDLAEEWFL ERVDASDLED NPVLAKAFED QVEGADYERA RQQNRPSRAD
RAFIDAKLEE AFDTDDEDDE EMLDLVDVRA PEEVEMTLAD LVLTTDQEDE IQKIVKAIEH
RDYLARIGLR EIGKLLFVGP PGTGKTSVAR ALAHDLDLPF VEVKLSMITS QYLGETAKNV
EKVFEVAKRL SPCILFMDEF DFVAKTRSSD EHAAIKRAVN TLLKSIDEIS LIQDEVLLIG
ATNHPDQLDA AAWRRFDEIV NFPKPDSGMR ADILRIVTQQ MEIDDFDPET LADLTEGLTG
SDLRLVLREA VLNALTEERT TLTQQDLEDA IIDFEERDNL KNMDMMDGDA DALVAGSGGF
SGDGGSDHDH DH
//
