ID D5V002_ARCNC Unreviewed; 442 AA.
AC D5V002;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Heat shock protein HslVU, ATPase subunit HslU {ECO:0000313|EMBL:ADG93614.1};
GN OrderedLocusNames=Arnit_1960 {ECO:0000313|EMBL:ADG93614.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93614.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG93614.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; CP001999; ADG93614.1; -; Genomic_DNA.
DR RefSeq; WP_013135759.1; NC_014166.1.
DR AlphaFoldDB; D5V002; -.
DR STRING; 572480.Arnit_1960; -.
DR KEGG; ant:Arnit_1960; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_7; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000000939; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 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; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Stress response {ECO:0000313|EMBL:ADG93614.1}.
FT DOMAIN 48..331
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 334..428
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 442 AA; 49993 MW; 65FF2CB392300469 CRC64;
MNMTPKEIVK FLDDYVIGQN DAKKTIALAL RNRYRRMQLA PEIQEEIMPK NILMIGSTGV
GKTEIARRLA KMMSLPFVKV EASKYTEVGF VGRDVESMIR DLVFASMDLV TKEYEEKIQD
GIEQEVNKQI IEKLVPHLPE GASESSKESF IKTFNKMEEK LLKGELEDKV IEIELPKKAH
VEVIDSSFPI DMTSMQESLN NMLGSLNKDK IKKEVKIKDA RKLLRSGASE KLIDQESIKH
EAIRRVENGG IIFIDEIDKI ASGKSNQNQD PSKEGVQRDL LPIVEGSNVQ TKYGQVKTDH
ILFIAAGAFH VSKPSDLLPE LQGRFPLRVE LNALDEEALY KILTNTKNSL LKQYKALLEV
EGVTLEFDDE AIHSFAHLSV EANQKAEDIG ARRLHTVIEK VLEDISFDAD EKNGETIIIT
KKLVEEKLSD IVKDEDTARY IL
//
