ID A0A0J8ATP2_9SPHN Unreviewed; 772 AA.
AC A0A0J8ATP2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:KMS57645.1};
GN Name=clpA {ECO:0000313|EMBL:KMS57645.1};
GN ORFNames=V473_05380 {ECO:0000313|EMBL:KMS57645.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS57645.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS57645.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS57645.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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:KMS57645.1}.
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; JACT01000001; KMS57645.1; -; Genomic_DNA.
DR RefSeq; WP_066601228.1; NZ_KQ130434.1.
DR AlphaFoldDB; A0A0J8ATP2; -.
DR STRING; 1420583.V473_05380; -.
DR PATRIC; fig|1420583.3.peg.1082; -.
DR Proteomes; UP000052232; 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:KMS57645.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KMS57645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052232};
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..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 85012 MW; 1D6DFE85D29FC4CD CRC64;
MPSFAPALET TLHNALTHAS ERKHEYATLE HLLLALIDDE HASKVMQACG VEIGELGDAV
TQYLDTELDS LKVEGSSDPS PTSGFQRVVQ RAILHVQSSG KDEVTGANVL VALFSERESY
AVYFLQQQDM SRLDAVSFIS HGVGKGTPTP ERQETKGASE EEKKVQDGKA KKDSALEQFT
VNLNEKAGRG KVDPLIGRTA EVDRTIQILC RRSKNNPLYV GDPGVGKTAI AEGLARKIVE
GEVPDVLKEA VIYSLDMGAL LAGTRYRGDF EERLKAVVTE LEKMPHAVLF IDEIHTVIGA
GATSGGAMDA SNLLKPALSG GTIRCIGSTT YKEFRNHFEK DRALLRRFQK IDVNEPTIED
TIKILAGLRT AFEEHHHVKY TPDAIKAAVE LSARYINDRK LPDKAIDVID EVGAMQMLVV
PSKRKKTITP KEIEQVIATM ARIPPKTVSS DDKTVLSSLT TDLKRVVFGQ DKAIEVLSSA
IKLSRAGLRD PDKPIGNYLF SGPTGVGKTE VARQLASIMG IPLQRFDMSE YMERHSVSRL
IGAPPGYVGY DQGGLLTDAV DQQPHSVLLL DEIEKAHPDL FNILLQVMDN GRLTDHHGKT
VDFRNTILIM TTNAGASDMA KESIGFGEFT REDVQEDAVK KLFTPEFRNR LDAIVPFDYL
PTEVVARVID KFVLQLELQL ADRDVHITLD QDAKDWLTKK GYDKLYGARP MGRLMQEKIK
QPLAEELLFG KLVHGGEVHV HMKDEALAFQ ITPAAPKKGK KGGKAKTTEG TK
//