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Database: UniProt
Entry: A0A163YUB8_9BRAD
LinkDB: A0A163YUB8_9BRAD
Original site: A0A163YUB8_9BRAD 
ID   A0A163YUB8_9BRAD        Unreviewed;       799 AA.
AC   A0A163YUB8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KZD22583.1};
GN   Name=clpA {ECO:0000313|EMBL:KZD22583.1};
GN   ORFNames=A4A58_29195 {ECO:0000313|EMBL:KZD22583.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD22583.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD22583.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD22583.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT   Fed.";
RL   Submitted (MAR-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:KZD22583.1}.
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DR   EMBL; LVYV01000020; KZD22583.1; -; Genomic_DNA.
DR   RefSeq; WP_068734397.1; NZ_LVYV01000020.1.
DR   AlphaFoldDB; A0A163YUB8; -.
DR   STRING; 943830.A4A58_29195; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000076574; 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:KZD22583.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KZD22583.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  87713 MW;  425B075EF54DA39A CRC64;
     MPTFSQSLEQ SLHRALSIAN ERHHQYATLE HLLLSLVDDS DAAAVMRACS VDLDKLRGSL
     VNYLETEFEN LVTDGADDAK PTAGFQRVIQ RAVIHVQSSG REEVTGANVL IAIFAERESH
     AAYFLQEQDM TRYDAVNYIS HGIAKRPGVS EARPVRGVDE ETETKNGDDA KKKGEALDTY
     CVNLNKKARD GKIDPVIGRT AEINRAIQVL CRRQKNNPLF VGEAGVGKTA IAEGLAKRIV
     DSDVPEVLSA ATVFSLDMGT LLAGTRYRGD FEERLKQVLK ELEAHPNAIL FIDEIHTVIG
     AGATSGGAMD ASNLLKPALA SGAIRCMGST TYKEYRQHFE KDRALVRRFQ KIDVNEPTVE
     DAISILKGLK PYFEDYHKLK YTNEAIEAAV QLSSRYIHDR KLPDKAIDVI DESGAAQMLV
     AESKRKKTIG IKEIETTIAT MARIPPKSVS KDDAEVLRHL ESTLKRVVFG QDKAIEALAA
     SIKLARAGLR EPEKPIGSYL FSGPTGVGKT EVAKQLASSL GVELIRFDMS EYMERHTVSR
     LIGAPPGYVG FDQGGLLTDG VDQHPHCVVL LDEIEKAHPD LYNVLLQVMD HGRLTDHNGK
     QVSFRNVILI MTTNAGAADM ARAAFGFTRG KREGEDQEAI NRQFAPEFRN RLDAVVSFAH
     LNSDVIGMVV EKFVLQLEAQ LADRDVTIEL SDPAKAWLIQ HGYDEQMGAR PMGRVIQEHI
     KKPLADELLF GKLKNGGHVR VVLKKDEAVL GVEQESIGFE FVDGPVTPKP EKLPAKRGAA
     KKPKSGKGSG SAKGPLEKA
//
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