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 12-APR-2017, entry version 89. DE RecName: Full=Protein ClpV1; GN Name=clpV1; OrderedLocusNames=PA0090; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / OS JCM 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 / RC 1C / 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., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic 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 / RC 1C / 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., RA Joachimiak A., Mekalanos J.J.; RT "A virulence locus of Pseudomonas aeruginosa encodes a protein RT secretion apparatus."; RL Science 312:1526-1530(2006). CC -!- FUNCTION: Required for secretion of hcp1 probably by providing the CC energy source for its translocation. CC {ECO:0000269|PubMed:16763151}. 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; NC_002516.2. DR PDB; 4UQW; X-ray; 1.50 A; A/B=1-161. DR PDBsum; 4UQW; -. DR ProteinModelPortal; Q9I742; -. DR SMR; Q9I742; -. DR IntAct; Q9I742; 1. DR STRING; 208964.PA0090; -. DR PaxDb; Q9I742; -. DR PRIDE; Q9I742; -. DR EnsemblBacteria; AAG03480; AAG03480; PA0090. DR GeneID; 879553; -. DR KEGG; pae:PA0090; -. DR PATRIC; 19834384; VBIPseAer58763_0094. DR PseudoCAP; PA0090; -. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR InParanoid; Q9I742; -. DR KO; K11907; -. DR OMA; LIVSRCT; -. 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:0019538; P:protein metabolic process; IEA:InterPro. DR Gene3D; 1.10.1780.10; -; 1. 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; IPR004176; Clp_N. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 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; PS00870; CLPAB_1; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Complete proteome; KW Cytoplasm; Nucleotide-binding; Reference proteome. FT CHAIN 1 902 Protein ClpV1. FT /FTId=PRO_0000250989. FT NP_BIND 237 244 ATP 1. {ECO:0000250}. FT NP_BIND 640 647 ATP 2. {ECO:0000250}. FT COILED 441 559 {ECO:0000255}. FT MUTAGEN 310 310 E->A: Loss of ATP hydrolytic activity and FT hcp1 secretion. FT {ECO:0000269|PubMed:16763151}. FT HELIX 6 10 {ECO:0000244|PDB:4UQW}. FT HELIX 15 31 {ECO:0000244|PDB:4UQW}. FT STRAND 34 36 {ECO:0000244|PDB:4UQW}. FT HELIX 38 47 {ECO:0000244|PDB:4UQW}. FT HELIX 52 59 {ECO:0000244|PDB:4UQW}. FT HELIX 64 77 {ECO:0000244|PDB:4UQW}. FT HELIX 90 105 {ECO:0000244|PDB:4UQW}. FT STRAND 110 112 {ECO:0000244|PDB:4UQW}. FT HELIX 114 122 {ECO:0000244|PDB:4UQW}. FT HELIX 125 134 {ECO:0000244|PDB:4UQW}. FT HELIX 136 140 {ECO:0000244|PDB:4UQW}. FT HELIX 143 148 {ECO:0000244|PDB:4UQW}. FT HELIX 150 154 {ECO:0000244|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 //