ID B3PL54_CELJU Unreviewed; 765 AA.
AC B3PL54;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=ATP-binding protease component ClpA {ECO:0000313|EMBL:ACE85625.1};
GN Name=clpA {ECO:0000313|EMBL:ACE85625.1};
GN OrderedLocusNames=CJA_2568 {ECO:0000313|EMBL:ACE85625.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85625.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85625.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85625.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000934; ACE85625.1; -; Genomic_DNA.
DR RefSeq; WP_012488164.1; NC_010995.1.
DR AlphaFoldDB; B3PL54; -.
DR STRING; 498211.CJA_2568; -.
DR KEGG; cja:CJA_2568; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001036; 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:ACE85625.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ACE85625.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
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 146..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 84586 MW; 5C7E6A191C329DF3 CRC64;
MLSKDLEVTL NLAFKGARSK RHEFMTVEHL LLALLDNDSA ANVLRACGAD LNGLRKELIE
FVDSTTPLIP EADTERETQP TLGFQRVLQR AVFHVQSSGK QEVTGANVLV AIFSEQESQA
VYYLKQQSIA RIDVVNYITH GIHKVAGHGD HQDHHQSSSP QESHEEESSS SESNSQSPLE
NFATNLNEAA MQGRIDPLVG REFEVERVCQ ILSRRRKNNP LLVGESGVGK TAIAEGLAKR
IVDGDVPEAL SDSVVYSLDM GALLAGTKYR GDFEKRFKSL LSELKKQRSS ILFIDEIHTI
IGAGAASGGV MDASNLLKPL LSSGEIRCMG STTFQEFRGI FDKDRALSRR FQKVDVNEPS
VEETYQILKG LKSRFEQHHN LRYTDAALRA AAELAERYIN DRFLPDKAID VIDEAGAYQQ
LQAPSKRKKT IGVGDVENVV AKIARIPPKN VSSSDKELLR KLDQNLKLTV FGQDEAIETL
ATAIKLSRAG LNSIEKPIGS FLFAGPTGVG KTEVCRQLAK CMAIDLVRFD MSEYMERHTV
SRLIGAPPGY VGFDQGGLLT DAITKQPHCV LLLDEIEKAH PEVFNLLLQV MDHGTLTDNN
GRKADFRNVI LVMTTNAGAE VMSRASIGFT HQDHTTDGME AIKKMFTPEF RNRLDAIIQF
APLALETIKT VVDKFLMELQ TQLDDKHVTL EISEDARQWL AIHGYDVKMG ARPMARLIQD
KLKKPLAEEI LFGSLSQGGG IVDVDLDPVE DKLSILIKAK QAQPA
//
