GenomeNet

Database: UniProt
Entry: A0A519QFW2_9SPHN
LinkDB: A0A519QFW2_9SPHN
Original site: A0A519QFW2_9SPHN 
ID   A0A519QFW2_9SPHN        Unreviewed;       800 AA.
AC   A0A519QFW2;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RZJ97561.1};
GN   Name=clpA {ECO:0000313|EMBL:RZJ97561.1};
GN   ORFNames=EOO76_18735 {ECO:0000313|EMBL:RZJ97561.1};
OS   Novosphingobium sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1874826 {ECO:0000313|EMBL:RZJ97561.1, ECO:0000313|Proteomes:UP000320223};
RN   [1] {ECO:0000313|EMBL:RZJ97561.1, ECO:0000313|Proteomes:UP000320223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PMG_125 {ECO:0000313|EMBL:RZJ97561.1};
RX   PubMed=30498029; DOI=.1073/pnas.1812668115;
RA   Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA   Murphy G.P., McGenity T.J., Murrell J.C.;
RT   "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
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:RZJ97561.1}.
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; SECS01000170; RZJ97561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A519QFW2; -.
DR   Proteomes; UP000320223; 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:RZJ97561.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZJ97561.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000320223};
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          144..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   800 AA;  87931 MW;  2C367C194025F1E6 CRC64;
     MPSFAQNLEK TLHSALAQAS ERSHEYATLE HLLLALIDDA DAAQVMEACG VDLGDLGDVV
     RQYLDQEYQS LKTQDKGDPA PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
     AVYFLQQQDM SRLDAVSFIS HGIGKGGRRI EDRTPKGNSE SETPQAEEKN ESKSQKKDSA
     LDQFTVNLNE KALTGKIDPL IGRGPEVDRT IQILCRRSKN NPLYVGDPGV GKTAIAEGLA
     RKIVEGEVPE VLTDAVIYSL DMGSLLAGTR YRGDFEERLK QVVSELEKMP EAVLFIDEIH
     TVIGAGATSG GAMDASNLLK PALSSGTIRC IGSTTYKEFR NHFEKDRALL RRFQKIDVNE
     PTIEDTIKIL KGLRSAFEDH HKVKYTPDAI KTAVELSARY INDRKLPDKA IDVIDEVGAM
     QMLVPPNKRK KTITAREIEQ VIATMARIPP KSVSSDDKKV LEHLDRDLKR VVFGQDKAVE
     KLSIAMKLSR AGLRDPDKPI GSFLFSGPTG VGKTEVAKQL AAIMGIPMQR FDMSEYMERH
     SVSRLIGAPP GYVGFDQGGL LTDAVDQQPH SVLLLDEIEK AHPDLFNILL QVMDNGRLTD
     HHGKTVDFRN VVLIMTTNAG ASDMAKQGIG FGDVSKEDAG DEAVKRMFTP EFRNRLDAIV
     PFSYLPTEVI SRVVDKFILQ LELQLADQNV HIQFDGDARG WLGERGYDKL YGARPMARLI
     QDKVKQPLAE ELLFGKLAHG GEVHVSVKDD ALNFELTPAP PKLVKRAAKG KAKVANPTAR
     AGRKPAAKKA SSSEPSTDGE
//
DBGET integrated database retrieval system