ID A0A0R2LBH2_9LACO Unreviewed; 744 AA.
AC A0A0R2LBH2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:KRN98801.1};
GN ORFNames=IV66_GL001785 {ECO:0000313|EMBL:KRN98801.1};
OS Ligilactobacillus pobuzihii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=449659 {ECO:0000313|EMBL:KRN98801.1, ECO:0000313|Proteomes:UP000051886};
RN [1] {ECO:0000313|EMBL:KRN98801.1, ECO:0000313|Proteomes:UP000051886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103219 {ECO:0000313|EMBL:KRN98801.1,
RC ECO:0000313|Proteomes:UP000051886};
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 ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:KRN98801.1}.
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DR EMBL; JQCN01000040; KRN98801.1; -; Genomic_DNA.
DR RefSeq; WP_017866814.1; NZ_JQCN01000040.1.
DR AlphaFoldDB; A0A0R2LBH2; -.
DR STRING; 449659.IV66_GL001785; -.
DR PATRIC; fig|449659.4.peg.1826; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051886; Unassembled WGS sequence.
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; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Hydrolase {ECO:0000313|EMBL:KRN98801.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KRN98801.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051886}.
FT DOMAIN 351..386
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 70..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 82417 MW; 6E590D5D259A45FB CRC64;
MLCQNCHQNP ATIHLTTSIN GRQTSIDLCQ NCYRKLKDQA GNTNNNRPSS MMQDPFGFGN
LDDIFRAMSS DQQGAQQQGQ VPPTQAAGGN GRNSGNNTIL GQYGLDLTSE AQNGRIDPVI
GRDKEIERVI EILNRRTKNN PVLIGEAGVG KTAVVEGLAQ KIVDNDVPQK LQNKKVIRLD
VVSLVQGTGI RGQFEERMKQ LMDEVKKAKD TILFIDEIHE IVGAGNAEGG MDAGNVLKPA
LARGDLQLVG ATTLNEYRTI EKDAALARRL QPVQVNEPSV EETVKILQGI SGRYEDYHHV
KFSEKALEAA ATLSDRYIQD RFLPDKAIDL LDEAGSKKNL TIHTVDPAVM DEKINQAEKE
KQAALKDEDY EKAAYYRDQV TKFKKMKDNS SSDEATPKIT DKDMEKIVEE KTDIPVGELK
AKEQSQLKNL ASSLENHVIG QDQAVTKVAR AIRRNRVGFN KSGRPIGSFL FVGPTGVGKT
ETAKQLAREL FGTEDAMIRF DMSEYMEKFS VSKLIGSPPG YVGYEEAGQL TEQVRRHPYS
LILLDEVEKA HPDVLHTFLQ ILDDGRLTDS QGRTVSFKDT IIIMTSNAGS GDSVASVGFG
AEASGQTHSI LDNLSKYFKP EFLNRFDGIV EFNALTKENL HHIVSLMLDE VNEMLANKGI
ELHVTGPVAD KLVDLGYDPK MGARPLRRVI QEQLEDKIAD YYLDDPSSQN LSARLEDGEI
KITKNDEPEK KTDTEKNDSA DKNE
//
