GenomeNet

Database: UniProt
Entry: A0A2K9LR95_9GAMM
LinkDB: A0A2K9LR95_9GAMM
Original site: A0A2K9LR95_9GAMM 
ID   A0A2K9LR95_9GAMM        Unreviewed;       753 AA.
AC   A0A2K9LR95;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AUM14770.1};
GN   Name=clpA {ECO:0000313|EMBL:AUM14770.1};
GN   ORFNames=Kalk_21085 {ECO:0000313|EMBL:AUM14770.1};
OS   Ketobacter alkanivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Ketobacter.
OX   NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM14770.1, ECO:0000313|Proteomes:UP000235116};
RN   [1] {ECO:0000313|Proteomes:UP000235116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA   Kim S.-J., Rhee S.-K.;
RT   "Direct submision.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP022684; AUM14770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9LR95; -.
DR   KEGG; kak:Kalk_21085; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000235116; 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; PS51903; CLP_R; 1.
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:AUM14770.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AUM14770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235116};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          149..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  83333 MW;  CAFCCF15050F295B CRC64;
     MLSKDLEVTL NLAFRDARTK RHEYMTVEHL LLALLDNEAA STVLKACGTD LDELRSDLAN
     FVDETTPLIP SSDSDRETQP TLGFQRVLQR AVFHVQSSGK KEVTGANVLV AIFSEQESQA
     VYFLKKQSVA RIDVVNYIAH GISKVSDETH NLEDHSHDVH EDDQVSEGAG KSPLEAYASN
     LNEQAMAGRI DPLVGRDEEV ERTVQILCRR RKNNPLLVGE PGVGKTAIAE GLAKRIVDKE
     VPDAIDDCVV FSLDLGALLA GTKYRGDFEK RFKALLAELQ KKSNAILFID EIHTIIGAGA
     ASGGVMDASN LLKPMLASGD IKCIGSTTFQ EYRGIFEKDR ALARRFQKID VVEPSVEDTF
     EILKGLKSRF EEHHDIKYSN KALKAACELS ARYINDRHLP DKAIDVIDEV GAYQRLLPPS
     KRKKVISVAD VEAIVSKIAR IPPKTVSAND KELLSNLERD LKMVVFGQND AIDALSSAIK
     LARAGLSHPD RPIGSFLFAG PTGVGKTEVT KQLAKVMGME LIRFDMSEYM ERHTVSRLIG
     APPGYVGFDQ GGLLTEAVTK SPHAVLLLDE IEKAHPEVFN LLLQVMDHGT LTDNNGRKAD
     FRNVILVMTT NAGAESVARA SIGFTQQDHT TDGMEAIKRM FTPEFRNRLD SVIQFHNLDM
     EIIKGVVDKF LTELQAQLDD KRVMLDVDDA ARNWLAEKGY DKDMGARPMN RLIQEKLKRP
     LAEKILFGEL SENGGTVHIS EEDGELIFDT EPA
//
DBGET integrated database retrieval system