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Database: UniProt
Entry: G9ZS66_9LACO
LinkDB: G9ZS66_9LACO
Original site: G9ZS66_9LACO 
ID   G9ZS66_9LACO            Unreviewed;       474 AA.
AC   G9ZS66;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=ATP-dependent protease HslVU, ATPase subunit {ECO:0000313|EMBL:EHL95846.1};
GN   ORFNames=HMPREF9103_02584 {ECO:0000313|EMBL:EHL95846.1};
OS   Lentilactobacillus parafarraginis F0439.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL95846.1, ECO:0000313|Proteomes:UP000004625};
RN   [1] {ECO:0000313|EMBL:EHL95846.1, ECO:0000313|Proteomes:UP000004625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0439 {ECO:0000313|EMBL:EHL95846.1,
RC   ECO:0000313|Proteomes:UP000004625};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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:EHL95846.1}.
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DR   EMBL; AGEY01000195; EHL95846.1; -; Genomic_DNA.
DR   RefSeq; WP_008214589.1; NZ_JH415059.1.
DR   AlphaFoldDB; G9ZS66; -.
DR   STRING; 797515.HMPREF9103_02584; -.
DR   PATRIC; fig|797515.3.peg.2329; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   Proteomes; UP000004625; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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   Hydrolase {ECO:0000313|EMBL:EHL95846.1};
KW   Protease {ECO:0000313|EMBL:EHL95846.1}.
FT   DOMAIN          51..364
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          363..462
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   474 AA;  53236 MW;  89509806D1CA1DE5 CRC64;
     MTESTQTPKQ IVEVLDQYII GQDEAKKAVA VALRNRYRRM QLSKAMQDEI SPKNLLMIGP
     TGVGKTEIAR RLAKIVNAPF VKVEATKFTE VGYVGGDVES MVRDLVENAI QLEREDEYKQ
     VRADAEKQAN NQLVKLLVPA QKKKNRQNDM QNLMNMFTQM QNGQTPTPEN QDDQEEVTDD
     IREKRMSVSD KLRAGLLEND QVEIEMDDPS QQASGQNTML NQMGIDLNDT LSGLMPKKKI
     KRTVPVSEAR EILIRQASEE LVNKADLYHN AIVRAENTGI IFIDEIDKIA PGNTKNSGEV
     SREGVQRDIL PIVEGSQVNT KYGPVNTDHM LFIGSGAFAE SKPSDLIPEL QGRFPIRVEL
     KDLTKDDFVR ILTEPTNSLT KQYIALIGTD NIKVTFTIEA VNRIAEIATE VNHNTDNIGA
     RRLHTILEKL LEDILYEGPD MQMGDITITE KYVDDKVGKL AGNKDLSRHS LNNH
//
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