ID A0A0R1VWG0_9LACO Unreviewed; 472 AA.
AC A0A0R1VWG0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP-dependent protease ATP-binding subunit HslU {ECO:0000313|EMBL:KRM08235.1};
GN ORFNames=FC89_GL001573 {ECO:0000313|EMBL:KRM08235.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM08235.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM08235.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM08235.1,
RC ECO:0000313|Proteomes:UP000051451};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM08235.1}.
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DR EMBL; AZGB01000001; KRM08235.1; -; Genomic_DNA.
DR RefSeq; WP_057870520.1; NZ_AZGB01000001.1.
DR AlphaFoldDB; A0A0R1VWG0; -.
DR STRING; 1423750.FC89_GL001573; -.
DR PATRIC; fig|1423750.3.peg.1616; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000051451; Unassembled WGS sequence.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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 ATP-binding {ECO:0000313|EMBL:KRM08235.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:KRM08235.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KRM08235.1};
KW Protease {ECO:0000313|EMBL:KRM08235.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051451}.
FT DOMAIN 51..365
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 364..458
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 472 AA; 52914 MW; 1F3DBB09BD5CC5FF CRC64;
MNPIDKTPKQ IVKELNNYVI GQNDAKKAIA VALRNRYRRL QLDAEMQAEI TPKNVLMIGP
TGVGKTEIAR RLAKIVAAPF IKVEATKFTE VGYVGRDVES MIRDLVEVAY KMEKEAEYQH
VHSQAVQEAD KQLIKLLVPA EKKQKQAESQ QNFMQMLRNL QAGNFDNLMP NQAQEENITD
EVRDQRLSVS EQLKKGLLEN RSVTIPVEDS SRSFQNQAGM LGQMGIDLGD ALSALTPTKK
VMRTMAVSQA REVLARQAAE KLIDSAEVAD RAIKRAEDTG IVFIDEIDKV TSKSKTNSGE
VSREGVQRDI LPIVEGSQVQ TKYGLLNTDH ILFIASGAFH ESKPSDLIAE LQGRFPIRVE
LDDLSTEDFV KILTEPSNAL IKQYMALIGT DNIKVTFTIE AIHRIAEIAY QVNHENENIG
ARRLHTILEK LLEDLLYEGP DMQMGDITIT EAYVEQKIGN IAKNKDLSQY IL
//
