ID A0A380U3W2_9PAST Unreviewed; 867 AA.
AC A0A380U3W2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease subunit B {ECO:0000313|EMBL:SUT95157.1};
GN Name=clpB_2 {ECO:0000313|EMBL:SUT95157.1};
GN ORFNames=NCTC10801_02403 {ECO:0000313|EMBL:SUT95157.1};
OS [Actinobacillus] rossii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae.
OX NCBI_TaxID=123820 {ECO:0000313|EMBL:SUT95157.1, ECO:0000313|Proteomes:UP000254649};
RN [1] {ECO:0000313|EMBL:SUT95157.1, ECO:0000313|Proteomes:UP000254649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10801 {ECO:0000313|EMBL:SUT95157.1,
RC ECO:0000313|Proteomes:UP000254649};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UFRQ01000003; SUT95157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380U3W2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000254649; 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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR001270; ClpA/B.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF182; CLP ATPASE; 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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SUT95157.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SUT95157.1}.
FT DOMAIN 214..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 599..765
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 765..857
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 867 AA; 97108 MW; 61329B4227E71CCC CRC64;
MKVELSSIIK KLSPVAKASL ENAALACMSD GLNEILVSHV LQQYLDTPLC DIRKILEYFQ
IDYIQLKDEI TKTQPILNSL EQGKYPAFSP LLLEALQDSW LISTAELGQN TLRTGAFLLA
LLESPMRYVL PQVANILINI NRDILKQQFM QITLGSVESD DISDAVQSKN AVNSEYLQKY
AQNLTELARQ GKIDPVLCRD NETNLIIDIL SRRRKNNPII VGEAGVGKSA LVEGLALRII
EGNVPDSLLN TEIMSLDLGA MQAGASVKGE FEKRFKGIIH EVTSSNSPII IFIDEAHTLI
GAGNQQGGLD VSNLLKPALA RGELKTIAAT TWGEYKKYIE KDAALSRRFQ MVKVEEPSVE
QSISILRGLQ SIYEKSHKVM IEEEALIASA KLSERYLTGR QLPDKAIDVL DTACARVAIN
LSSPPKLLSS YQNEKYQKEM EISLLEREIA IGISKDESRL KQLKSDLLKL DGKRFSLNEK
WEKQKELVKQ VIELRENVLH SEEKDLAKLK KLKTLNSKLI KLQSNDLLVS AQVTKKEIES
VIAEWTGVPL DKLSQNELYA VTHLPELLND EIKGQELAIH HLYKHLLTAR ADLRRLGRPL
GSFLLVGPSG VGKTETVLQI TDLLFGGKQY LTTINMSEFQ EKHTVSRLIG SPPGYVGYGE
GGVLTEAIRR KPYSVVLLDE VEKAHPDVLN LFYQAFDKGE LADGEGRVID CKNIVFFLTS
NLGYQTIVEY KDNPVEMQNA LYPVLADFFK PALLARMEIV PYLPLEQETL RIIVNGKLAK
LSKLLEKRFN AKVHIDEDVR IEILSRVSRM ENGARILESI IDGQLLPPVS LLLLQAIANK
QDVTEIHFFV KNNQFFARVG EQECDVN
//