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
//