ID A0A2T6B6L7_9RHOB Unreviewed; 773 AA.
AC A0A2T6B6L7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PTX51729.1};
GN ORFNames=C8N34_103232 {ECO:0000313|EMBL:PTX51729.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX51729.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX51729.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX51729.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX51729.1}.
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; QBKP01000003; PTX51729.1; -; Genomic_DNA.
DR RefSeq; WP_054301717.1; NZ_VLLH01000002.1.
DR AlphaFoldDB; A0A2T6B6L7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244224; 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:PTX51729.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PTX51729.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 148..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 85052 MW; 98E482EC48DFA571 CRC64;
MPSFSTTLEQ AIHAALAIAN ARRHELATLE HLLLALIDEP EAARVMKACS VDLDDLRKTL
TDFIDDDLST LVTSVEGSEA VPTAAFQRVI QRAAIHVQSS GRSEVTGANV LVAIFAERES
NAAYFLQEQD MTRYDAVNFI AHGVAKDPSY GESRPVSGSE EHQHETPKGE AGEAKESALS
KYCVDLNVKA RMGDVDPLIG REGEVERCIQ VLCRRRKNNP LLVGDPGVGK TAIAEGLAKK
IVDGETPEIL AHATIYSLDM GALLAGTRYR GDFEERLKAV VKEMEDHPDA ILFIDEIHTV
IGAGATSGGA MDASNLLKPA LQGGKLRCMG STTYKEFRQH FEKDRALSRR FQKIDVNEPS
VPDAIKILQG LKPHFEQHHD LRYTNEAIKS AVELAARYIN DRKLPDSAID VIDEAGAAQH
LVAANKRRKT IGIREIEAVV AKIARIPPKT VSKDDAEVLR DLEKTLKRVV FGQDKAIEAL
SASIKLARAG LREPEKPIGN YLFAGPTGVG KTEVAKQLAS TLGVELLRFD MSEYMEKHAV
SRLIGAPPGY VGFDQGGMLT DGVDQHPHCV LLLDEIEKAH PDVYNILLQV MDHGKLTDHN
GRQVDFRNVI LIMTTNAGAS DMQRAAIGFG RDKRQGEDTA AIERTFTPEF RNRLDAVIAF
APLTKETIMQ VVEKFVLQLE AQLMDRNVHI ELSDEAARWL GDKGYDDKMG ARPLGRVIQE
HLKKPLAEEL LFGRLQKGGV VRVKVKDDRI DLIIEEPGKP QLTGQKPPLL TAE
//