CLPV1_PSEAE
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 03-AUG-2022, entry version 106.
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}.
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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 AlphaFoldDB; Q9I742; -.
DR SMR; Q9I742; -.
DR IntAct; Q9I742; 1.
DR STRING; 287.DR97_3047; -.
DR PaxDb; Q9I742; -.
DR PRIDE; 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 BioCyc; PAER208964:G1FZ6-92-MON; -.
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 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 BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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
