ID A0A0Q4MLA8_9GAMM Unreviewed; 758 AA.
AC A0A0Q4MLA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KQN56850.1};
GN Name=clpA {ECO:0000313|EMBL:KQN56850.1};
GN ORFNames=ASF13_06970 {ECO:0000313|EMBL:KQN56850.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN56850.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN56850.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56850.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN56850.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56850.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN56850.1}.
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DR EMBL; LMLK01000021; KQN56850.1; -; Genomic_DNA.
DR RefSeq; WP_056236918.1; NZ_LMLK01000021.1.
DR AlphaFoldDB; A0A0Q4MLA8; -.
DR STRING; 1736225.ASF13_06970; -.
DR Proteomes; UP000050856; 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:KQN56850.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KQN56850.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 140..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83969 MW; 1FF64C7184AEE462 CRC64;
MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACTVD IVALRQELEA
FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR SEVAGANVLV AIFSEQESQA
AYLLRKHEVS RLDVVNFISH GTRKDEPGPS ASAENPVNEE QAGGEDRMEN FTTNLNQLAR
VGGIDPLIGR DKELERTVQV LCRRRKNNPL LVGESGVGKT AIAEGLAWRI VQGDVPEVMQ
DCTIYSLDIG SLLAGTKYRG DFEKRFKALL KQLEQDTNSI LFIDEIHTII GAGAASGGQV
DAANLIKPLL SGGKIRVMGS TTYQEFSNIF EKDRALARRF QKIDITEPSV DETVQIINGL
KPKYEAHHDV RYTAKAIRAA VELAVKYIND RHLPDKAIDV IDEAGARARL MPVSKRKKTV
NVADIESVVA RIARIPEKSV SATDRDTLRT LGDRLKMLVF GQDNAIEALT EAIKMSRAGL
GQDRKPVGSF LFAGPTGVGK TEVTVQLAKA LGIELLRFDM SEYMERHTVS RLIGAPPGYV
GFDQGGLLTD AVIKHPHAVV LLDEIEKAHP DVFNLLLQVM DNGMLTDNNG RKADFRNVVV
VMTTNAGVRE TERKSIGLIQ QDNSTDAMEE IKKIFTPEFR NRLDNIIWFR HLDQVVIHQV
VDKFIVELQA QLDAKGVSLE VSDDARNWLA EKGYDKAMGA RPMARTVQES LKKPLANELL
FGSLVEGGSV SVTLDKENNQ LAYHFLSAAK RKAEGTVH
//
