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Database: UniProt
Entry: A0A0Q4LB53_9SPHN
LinkDB: A0A0Q4LB53_9SPHN
Original site: A0A0Q4LB53_9SPHN 
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
//
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