GenomeNet

Database: UniProt
Entry: A0A5E7YES1_9SPHN
LinkDB: A0A5E7YES1_9SPHN
Original site: A0A5E7YES1_9SPHN 
ID   A0A5E7YES1_9SPHN        Unreviewed;       793 AA.
AC   A0A5E7YES1;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   SubName: Full=ATPase and specificity subunit of ClpA-ClpP ATP-dependent serine protease, chaperone activity {ECO:0000313|EMBL:VVT03742.1};
GN   Name=clpA {ECO:0000313|EMBL:VVT03742.1};
GN   ORFNames=ERY430_41003 {ECO:0000313|EMBL:VVT03742.1};
OS   Erythrobacter sp. EC-HK427.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=2038396 {ECO:0000313|EMBL:VVT03742.1, ECO:0000313|Proteomes:UP000325427};
RN   [1] {ECO:0000313|EMBL:VVT03742.1, ECO:0000313|Proteomes:UP000325427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERY430 {ECO:0000313|EMBL:VVT03742.1};
RA   Dittami M. S.;
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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; CABVLF010000004; VVT03742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5E7YES1; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000325427; 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:VVT03742.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:VVT03742.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325427};
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..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  86859 MW;  F475880ED79E3E90 CRC64;
     MPSFAQNLEK TLHNAIQHAI DRAHEYATLE HLLLALVSDS DAAEVMNACG VDLEELTGVV
     RQYLDQEYQS LKTEEDADPQ PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
     AVYFLQQQDM SRLDAVSFIS HGIGKGGKQI ESRTPEGAED EAQAPADEKG EKKKDSALDQ
     FCVNLNQKAL DGRIDPLIGR GPEVDRTVQI LCRRSKNNPL YVGDPGVGKT AIAEGLARKI
     VEGDVPEVLE PAVIYALDMG ALLAGTRYRG DFEERLKQVV NELEKMPDAV LFIDEIHTVI
     GAGATSGGAM DASNLLKPAL SSGAIRCIGS TTYKEFRNHF EKDRALLRRF QKIDVNEPTI
     EDTIKILKGL RSAFEEHHKV KYTPDAIKTA VEMSARYIND RKLPDKAIDV IDEVGAMQML
     VPPSRRRKTI TAKEIEKVVA TMARIPPKSV SKDDKAALST LEKDLKRVVF GQDEAIERLS
     VAMKLSRAGL RDPDKPIGSF LFSGPTGVGK TEVARQLASI MGIELKRFDM SEYMERHSVS
     RLIGAPPGYV GYDQGGLLTD AIDQHPHCVL LLDEIEKAHP DLFNILLQVM DNGKLTDHHG
     KTVDFRNVVL IMTTNAGASD AAKQGIGFGA GQKTEASEEA VKKMFTPEFR NRLDAIVPFA
     YLAPDTISRV VDKFILQLEL QLAEQNVHIQ FDGDAREWLG KRGYDKLMGA RPMARLIQEK
     VKQPLAEELL FGKLASGGEV HVSVKDEKLA FELTPAAPKS KAKPKRKASA KKAAPKASGS
     PAAGEDDGTA SEG
//
DBGET integrated database retrieval system