ID A0A0Q4LB53_9SPHN Unreviewed; 772 AA.
AC A0A0Q4LB53;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KQN31649.1};
GN Name=clpA {ECO:0000313|EMBL:KQN31649.1};
GN ORFNames=ASF00_02320 {ECO:0000313|EMBL:KQN31649.1};
OS Sphingomonas sp. Leaf34.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN31649.1, ECO:0000313|Proteomes:UP000051932};
RN [1] {ECO:0000313|EMBL:KQN31649.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31649.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN31649.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31649.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQN31649.1}.
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DR EMBL; LMLC01000001; KQN31649.1; -; Genomic_DNA.
DR RefSeq; WP_055873559.1; NZ_LMLC01000001.1.
DR AlphaFoldDB; A0A0Q4LB53; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051932; Unassembled WGS sequence.
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:KQN31649.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KQN31649.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 143..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 84528 MW; A014B01C19C961A2 CRC64;
MPSFAPALET TLHKALEAAS ARRHEYATLE HLLLALIDDE HASKVMTACN VEIGELKNTV
AHYLDSELDA LKVDAATDPS PTSGFQRVVQ RAILHVQSSG RDEVTGANVL VALFSERESY
AVYFLQQQDM SRLDAVSFIS HGVGKGGQQP TEASTPKGAD DEKPAKGQEK GKTESALKQF
TVDLNEKAKN GKVDPLIGRG PEVDRTIQIL CRRSKNNPLY VGDPGVGKTA IAEGLARKIV
EGDVPDVLLP AIIYSLDMGA LLAGTRYRGD FEERLKAVVN ELEKLPDAVL FIDEIHTVIG
AGATSGGAMD ASNLLKPALS GGTIRCIGST TYKEFRNHFE KDRALLRRFQ KIDVNEPTIE
DTIKILAGLR SAFEDHHNVK YTPDAIKSAV ELSARYINDR KLPDKAIDVI DEVGAMQMLV
PPNKRKKTIT PKEIEQVIAT MARIPPKSVS TDDKLALATL ETDLKRVVFG QNAAIEKLSS
AIKLARAGLR EPEKPIGNYL FTGPTGVGKT EVAKQLSTIL GIPLQRFDMS EYMERHSVSR
LIGAPPGYVG FDQGGLLTDA VDQNPHCVLL LDEIEKAHPD LFNILLQVMD NGRLTDQHGK
SVDFRNVILI MTTNAGASDM ARETVGFGNL TREGEDEQAV QKMFTPEFRN RLDAVVPFGY
LPTEVVARVV DKFILQLELQ LADRGVHIML DEESKAWLTT KGYDKLYGAR PMGRLIQEKI
KQPLAEELLF GKLVHGGEVT VKMKDGALAF AIEPAAPKKP KKKGKVESVD AK
//