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Database: UniProt
Entry: A0A1V2EU23_9SPHN
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ID   A0A1V2EU23_9SPHN        Unreviewed;       773 AA.
AC   A0A1V2EU23;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:ONF95808.1};
GN   Name=clpA {ECO:0000313|EMBL:ONF95808.1};
GN   ORFNames=SPHI_20100 {ECO:0000313|EMBL:ONF95808.1};
OS   Sphingomonas jeddahensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1915074 {ECO:0000313|EMBL:ONF95808.1, ECO:0000313|Proteomes:UP000188729};
RN   [1] {ECO:0000313|EMBL:ONF95808.1, ECO:0000313|Proteomes:UP000188729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G39 {ECO:0000313|EMBL:ONF95808.1,
RC   ECO:0000313|Proteomes:UP000188729};
RA   Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Sphingomonas jeddahensis G39.";
RL   Submitted (NOV-2016) 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:ONF95808.1}.
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DR   EMBL; MPSB01000008; ONF95808.1; -; Genomic_DNA.
DR   RefSeq; WP_076744777.1; NZ_MPSB01000008.1.
DR   AlphaFoldDB; A0A1V2EU23; -.
DR   STRING; 1915074.SPHI_20100; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000188729; 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:ONF95808.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ONF95808.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188729};
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          146..177
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   773 AA;  84852 MW;  7585659431291DC5 CRC64;
     MPSFASALET TLHKALEAAS SRRHEYATLE HLLFALVDDE HASQVMTACG VDLGEIKTTV
     AHYLDTELGA LKVDQQTDPS PTSGFQRVVQ RAILHVQSSG RDEVTGANVL VALFSERESY
     AVYFLQQQDM SRLDAVSFIS HGVGKGVSTP ETAASPKGAE DKEEKKPAEK GAKGESALKQ
     FTVDLNEKAK NGKVDPLIGR GPEVDRTVQI LCRRSKNNPL YVGDPGVGKT AIAEGLARKI
     VEGDVPDVLK PAVIYSLDMG ALLAGTRYRG DFEERLKQVV NELEKLPDAV LFIDEIHTVI
     GAGATSGGAM DASNLLKPAL SGGTIRCIGS TTYKEFRNHF EKDRALLRRF QKIDVNEPTI
     EDTIKILAGL RSAFETHHDV KYTPDAIKSA VELSARYIND RKLPDKAIDV IDEVGAMQML
     VAPSKRKKTI TPKEIEQVIA TMARIPPKSV STDDKKVLET LDTDLKRVVF GQNKAIENLS
     SAIKLSRAGL RDPEKPIGNY LFTGPTGVGK TEVAKQLATI MGIPLQRFDM SEYMERHSVS
     RLIGAPPGYV GFDQGGLLTD AVDQNPHCVL LLDEIEKAHP DLFNILLQVM DNGRLTDQHG
     KTVDFRNVIL IMTTNAGASD MARETLGFGN LSREGEDEQA VQRLFTPEFR NRLDAIVPFS
     YLPTEVVSRV VDKFILQLEL QLADRDVHIK LDDEARQWLT AKGYDKLYGA RPMGRLIQEK
     IKQPLAEELL FGKLVHGGEV VVKLKDNALA FEIVGAAPKK PKRKGGKAKV VAE
//
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