ID A0A0W0XS17_9GAMM Unreviewed; 755 AA.
AC A0A0W0XS17;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP binding protease component ClpA {ECO:0000313|EMBL:KTD47332.1};
GN ORFNames=Lrub_2254 {ECO:0000313|EMBL:KTD47332.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD47332.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD47332.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD47332.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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:KTD47332.1}.
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DR EMBL; LNYT01000020; KTD47332.1; -; Genomic_DNA.
DR RefSeq; WP_058532205.1; NZ_LNYT01000020.1.
DR AlphaFoldDB; A0A0W0XS17; -.
DR STRING; 458.Lrub_2254; -.
DR GeneID; 48947041; -.
DR PATRIC; fig|458.5.peg.2351; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000054608; 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:KTD47332.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KTD47332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054608};
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"
SQ SEQUENCE 755 AA; 83913 MW; 1374A042434E09DB CRC64;
MLNKELEFTL NLAFKEAKEK RHEFMTVEHL LLSLLDNPAA GNVLQACDAN IDALRRDLIE
FIDETTPRIP DDELDRETQP TLGFQRVLQR AVFHVQSAGK TEVTGANVLA AIFSEQESQA
VYFLRRENIT RLDVINYISH GVSKYHNNDL NEGMNSSMDE EMMSGEGTES PLESYCTNLN
KRARMGKIDP LIGRHEEIQR TIQVLCRRRK NNPLLVGEAG VGKTAIAEGL ARRIVDGEVP
EAIQNCIVYS LDLGALLAGT KYRGDFEKRL KAVLKQLGHQ EGAVLFIDEI HTIIGAGAAS
GGVMDASNLI KPLLANGELK CIGSTTYQEY RGIFEKDRAL ARRFQKIDIT EPSVEETFEI
LKGLKGRLEE HHGVKFSIPA LKAAAELSAK YINDRFLPDK AIDVVDEAGA YQNLLTANKR
RKIISVTEIE SVVAKIARIP VKKVSARDKD TLRNLERDLK LLVYGQDIAI TALASAIKLA
RSGLREPQKP VGCFLFAGPT GVGKTEVTRQ LANVLGIELL RFDMSEYMEK HTVSRLIGAP
PGYVGYDQGG LLTEAVTKNP HSVLLLDEIE KAHPDVFNLL LQIMDHGTLT DTNGRQADFR
HVILVMTSNA GASEISRNSI GFSLQDNSND GLEVIKRQFS PEFRNRLDAI INFAPLDNVT
IGLVVDKFIM ELDEQLSNKG VTFKVDKAAR EWLIEHGYDK AMGARPMARL IQENIKKPLA
DELLFGKLSN GGHVTLKVKD GKLHFDSHDY REGVC
//