ID A0A0M2K7T8_9GAMM Unreviewed; 758 AA.
AC A0A0M2K7T8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KKF34989.1};
GN Name=clpA {ECO:0000313|EMBL:KKF34989.1};
GN ORFNames=SY86_05380 {ECO:0000313|EMBL:KKF34989.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF34989.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF34989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF34989.1};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-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:KKF34989.1}.
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; JXNU01000003; KKF34989.1; -; Genomic_DNA.
DR RefSeq; WP_016189683.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2K7T8; -.
DR STRING; 65700.SY86_05380; -.
DR PATRIC; fig|65700.7.peg.1349; -.
DR Proteomes; UP000033924; 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:KKF34989.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKF34989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033924};
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 141..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84166 MW; 9284034FCA3983E4 CRC64;
MLNQELELSL NMTFARAREH RHEFMTVEHL LLALLSNSSA RETLEACNVD IVALRQELEA
FIEQTTPVLP VSAEERDTQP TLSFQRVLQR AVFHVQSSGR SEVAGANVLV AIFSEQESQA
AYLLRKYEIS RLDAVNFISH GTRKDEPGAS ASSDNPVNEE QAGGEERMEN FTTNLNQLAR
VGEIDPLIGR DKELERAVQV LCRRRKNNPL LVGESGVGKT AIAEGLAWRI VQGDVPEVMK
DATIYSLDIG SLLAGTKYRG DFEKRFKALL KQLEQDNSSI LFIDEIHTII GAGAASGGQV
DAANLIKPLL SGGKIRVMGS TTYQEFSNIF EKDRALARRF QKIDITEPSM DETVQIINGL
KPKYETHHEV RYTAKAVRAA VELSVKYIND RHLPDKAIDV IDEAGARARL IPVSKRKKTV
NVSDIESVVA RIARIPEKSV SATDRDTLRT LGDRLKMLVF GQDNAIETLT EAIKMSRAGL
GQDRKPVGSF LFAGPTGVGK TEVTVQLAKA LGIELLRFDM SEYMERHTVS RLIGAPPGYV
GFDQGGLLTD AVIKHPHAVV LLDEIEKAHP DVFNLLLQVM DNGMLTDNNG RKADFRNVVV
VMTTNAGVRE TERKSIGLIQ QDNSTDAMEE IKKIFTPEFR NRLDNIIWFK HLDLEVIHQV
VDKFIVELQA QLDAKGVSLE VSDEARDWLA EKGYDKAMGA RPMARTVQEN LKKPLANELL
FGSLVDGGSV SVALDKAKNE LTYHFLSAEK RKTEGTVH
//
