ID CLPV1_PSEAE Reviewed; 902 AA. AC Q9I742; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-FEB-2022, entry version 104. DE RecName: Full=AAA+ ATPase ClpV1; GN Name=clpV1; OrderedLocusNames=PA0090; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / RC PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [2] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-310. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / RC PRS 101 / PAO1; RX PubMed=16763151; DOI=10.1126/science.1128393; RA Mougous J.D., Cuff M.E., Raunser S., Shen A., Zhou M., Gifford C.A., RA Goodman A.L., Joachimiak G., Ordonez C.L., Lory S., Walz T., Joachimiak A., RA Mekalanos J.J.; RT "A virulence locus of Pseudomonas aeruginosa encodes a protein secretion RT apparatus."; RL Science 312:1526-1530(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-161, INTERACTION WITH TAGJ, AND RP FUNCTION. RX PubMed=25305017; DOI=10.1074/jbc.m114.600510; RA Foerster A., Planamente S., Manoli E., Lossi N.S., Freemont P.S., RA Filloux A.; RT "Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the RT accessory protein TagJ/HsiE1 distinguishes type VI secretion classes."; RL J. Biol. Chem. 289:33032-33043(2014). CC -!- FUNCTION: Component of the H1 type VI (H1-T6SS) secretion system that CC plays a role in the release of toxins targeting both eukaryotic and CC prokaryotic species. Acts as an AAA(+) ATPase that disassembles the CC contracted sheath, which resets the systems for reassembly of an CC extended sheath that is ready to fire again. CC {ECO:0000269|PubMed:16763151, ECO:0000269|PubMed:25305017}. CC -!- SUBUNIT: Interacts with TagJ. {ECO:0000269|PubMed:25305017}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16763151}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}. 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; AE004091; AAG03480.1; -; Genomic_DNA. DR PIR; G83635; G83635. DR RefSeq; NP_248780.1; NC_002516.2. DR RefSeq; WP_003115056.1; NZ_QZGE01000015.1. DR PDB; 4UQW; X-ray; 1.50 A; A/B=1-161. DR PDBsum; 4UQW; -. DR SMR; Q9I742; -. DR IntAct; Q9I742; 1. DR STRING; 287.DR97_3047; -. DR PaxDb; Q9I742; -. DR EnsemblBacteria; AAG03480; AAG03480; PA0090. DR GeneID; 879553; -. DR KEGG; pae:PA0090; -. DR PATRIC; fig|208964.12.peg.94; -. DR PseudoCAP; PA0090; -. DR HOGENOM; CLU_005070_1_1_6; -. DR InParanoid; Q9I742; -. DR OMA; PDMSREF; -. DR PhylomeDB; Q9I742; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR017729; ATPase_T6SS_ClpV1. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR036628; Clp_N_dom_sf. DR InterPro; IPR004176; Clp_R_dom. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR041546; ClpA/ClpB_AAA_lid. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF17871; AAA_lid_9; 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; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR TIGRFAMs; TIGR03345; VI_ClpV1; 1. DR PROSITE; PS51903; CLP_R; 1. DR PROSITE; PS00870; CLPAB_1; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm; KW Nucleotide-binding; Reference proteome; Repeat. FT CHAIN 1..902 FT /note="AAA+ ATPase ClpV1" FT /id="PRO_0000250989" FT DOMAIN 10..151 FT /note="Clp R" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251" FT NP_BIND 237..244 FT /note="ATP 1" FT /evidence="ECO:0000250" FT NP_BIND 640..647 FT /note="ATP 2" FT /evidence="ECO:0000250" FT REGION 13..78 FT /note="Repeat 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251" FT REGION 88..151 FT /note="Repeat 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251" FT COILED 441..559 FT /evidence="ECO:0000255" FT MUTAGEN 310 FT /note="E->A: Loss of ATP hydrolytic activity and hcp1 FT secretion." FT /evidence="ECO:0000269|PubMed:16763151" FT HELIX 6..10 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 15..31 FT /evidence="ECO:0007829|PDB:4UQW" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 38..47 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 52..59 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 64..77 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 90..105 FT /evidence="ECO:0007829|PDB:4UQW" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 114..122 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 125..134 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 136..140 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 143..148 FT /evidence="ECO:0007829|PDB:4UQW" FT HELIX 150..154 FT /evidence="ECO:0007829|PDB:4UQW" SQ SEQUENCE 902 AA; 98738 MW; DB45A33B091C0071 CRC64; MSEISRVALF GKLNSLAYKA IEAATVFCKL RGNPYVELVH WFHQILQLPD SDLHQIVRQS GIDPARLAKD LTEALDRLPR GSTSITDLSS HVEEAVERGW VYGSLMFGES QVRTGYLVIG ILKTPSLRHA LTGLSAEFAK LKVEALTERF DEYVGASPEN GLSASDGFNA GAAPGEASGA LAPSAMGKQE ALKRFTVDLT EQARSGKLDP IVGRDEEIRQ LVDILMRRRQ NNPILTGEAG VGKTAVVEGF ALRIVAGDVP PALKDVELRA LDVGLLQAGA SMKGEFEQRL RQVIEDVQSS EKPIILFIDE AHTLVGAGGA AGTGDAANLL KPALARGTLR TVAATTWAEY KKHIEKDPAL TRRFQVVQVD EPSEHKAILM MRGVASTMEK HHQVQILDEA LEAAVRLSHR YIPARQLPDK SVSLLDTACA RTAISLHAVP AEVDDSRRRI EALETELAII RRESAIGVAT AERQRNAETL LAEERERLAA LEQRWAEEKR LVDELLETRA RLRAAAEAVD AGGVPLGEGE VRLDEEQRQA LHARLAELQA QLSALQGEEP LILPTVDYQA VASVVADWTG IPVGRMARNE IETVLNLDRH LKKRIIGQDH ALEMIAKRIQ TSRAGLDNPS KPIGVFMLAG TSGVGKTETA LALAEAMYGG EQNVITINMS EFQEAHTVST LKGAPPGYIG YGEGGVLTEA VRRKPYSVVL LDEVEKAHPD VHEIFFQVFD KGVMEDGEGR VIDFKNTLIL LTTNAGTEMI ASLCADPELM PEPEAIAKSL REPLLKIFPP ALLGRLVTIP YYPLSDDMLK AISRLQLGRI KKRVEATHKV PFEFDEGVVD LIVSRCTETE SGGRMIDAIL TNTLLPDMSR EFLTRMLEGK PLAGVRISSR DNQFHYDFAE AE //