ID A0A0N7KBK5_9GAMM Unreviewed; 741 AA.
AC A0A0N7KBK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:BAS68271.1};
GN Name=clpA {ECO:0000313|EMBL:BAS68271.1};
GN ORFNames=BSEPE_1287 {ECO:0000313|EMBL:BAS68271.1};
OS endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS68271.1, ECO:0000313|Proteomes:UP000067399};
RN [1] {ECO:0000313|EMBL:BAS68271.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS68271.1,
RC ECO:0000313|Proteomes:UP000067399};
RA Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT mussels: influence on host distributions.";
RL Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN [2] {ECO:0000313|EMBL:BAS68271.1, ECO:0000313|Proteomes:UP000067399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS68271.1,
RC ECO:0000313|Proteomes:UP000067399};
RX PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA Hirano T., Maruyama T., Yoshida T.;
RT "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT symbiont population.";
RL ISME J. 10:990-1001(2016).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AP013042; BAS68271.1; -; Genomic_DNA.
DR RefSeq; WP_066045314.1; NZ_AP013042.1.
DR AlphaFoldDB; A0A0N7KBK5; -.
DR STRING; 1303921.BSEPE_1287; -.
DR KEGG; ebh:BSEPE_1287; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000067399; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR013461; ClpA.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Hydrolase {ECO:0000313|EMBL:BAS68271.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAS68271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067399};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 202..346
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 483..650
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 649..738
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 741 AA; 82637 MW; E55FFAB8A60ED0B8 CRC64;
MIEAGLQQEI NYIMTKARNN RLEFVTVEHL LIALFNIDEV VSFLRNKQVN LEEFRADLED
YIDSNTPLIP QQSEIDIVPT VGFQRVLQRS VYQAQSAQKN TVYAMNILVS IFSEKESYAV
YLLKQNGVSR LEVMEAMSTQ TAAYTDDDRD YKTDAKPKKK NKNALETYTT NLCEKSKSGK
IDPLLGREEE VLRTVQILSR RRKNNPLFVG QAGVGKTAIA QGIAKKIVDG KVPEVLKNAS
IYSLDVGVLV AGTKYRGDFE KRLKSVLSDL EKIPDAILFI DEIHTIVGAG SVSGGSLDAS
NLLKPALADG TLKCMGSTTY EEYRKVFEKD HALSRRFQKI DIDEPSVDDT IKILNGLKEA
YQTHHKVKYS KASLVSAVEL SHRYMNDRRL PDKAIDVIDE VGALQQIQPK SKRKVNIGVG
DIEDIVAKLA RIPSRQVTKD DKSLLKSLEA DLKLGVFGQE KAVESLSTAI KLSRSGLAHE
DKPMGSFLFA GPTGVGKTEI CKQLARIMGV KLLRFDMSEY MERHSISKLV GSPPGYVGYD
EGGLLTEAVN ANPYAVLLLD EVEKAHPDIF NLLLQVMDNG KLTDANGREV DFSNVILVMT
SNIGAQSVGR ASIGFNEQDH SLDYEGELKK AFTPEFRNRL SEVIYFNSLN EKTIVFVVNK
FLFELESALE DKNVSLIVSE TSRKWFAKNG YDAKMGARPM SRLIEKEIRK PLADELLFGK
LVTGGTVKVE IKKDKITLTI K
//