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Database: UniProt
Entry: A0A0N7KBK5_9GAMM
LinkDB: A0A0N7KBK5_9GAMM
Original site: A0A0N7KBK5_9GAMM 
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
//
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