ID A0A0D5NPB4_9BACL Unreviewed; 499 AA.
AC A0A0D5NPB4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATPase {ECO:0000313|EMBL:AJY77129.1};
GN ORFNames=VN24_24510 {ECO:0000313|EMBL:AJY77129.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY77129.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY77129.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY77129.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
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DR EMBL; CP011058; AJY77129.1; -; Genomic_DNA.
DR RefSeq; WP_045672554.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NPB4; -.
DR STRING; 1126833.VN24_24510; -.
DR KEGG; pbj:VN24_24510; -.
DR PATRIC; fig|1126833.4.peg.5392; -.
DR HOGENOM; CLU_000688_16_2_9; -.
DR Proteomes; UP000032633; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032633}.
FT DOMAIN 102..246
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 499 AA; 54761 MW; 39D4B8799BDD0968 CRC64;
MRKYKWEILA GFVPVLLLFL LTRGINILPI VFAILMAGGI FYVLRSRGQL AAAGGARESK
GKAPAVLSFD DIGGQERPKQ ELIEALDFLV RHEEIAKFGI RPLKGILLTG PPGTGKTLLA
KAAAHYTDSI YVAASGSEFV EMYVGVGAGR IRDLFKEARK KASKAGKASA VIFIDEIDVI
GGKRDGGQHR EYDQTLNQLL TEMDGIHTNE SPRILLIAAT NRKEMLDSAL LRPGRFDRHI
GVDLPDKKGR LHILNIHGRN KPLAKDASLE RVAEESFGFS GAQLESVMNE AAIYALREAK
PLIGQQHLSM AIDKVMMGEK TDREATNEER ERVAIHELGH AIAAEMVRPG SVSQVALSPR
GQALGYVRHN PQQDRYLYTQ DFLEAQIMIA LGGAAAEEMF YGGRSTGSRG DFDQAMSIVR
TMVESGLTEL GIIDASMMTP DGWAKVTSSI LDGLMDRTKR MLAEQRDLFM HSLGILITEE
TLHGDRFRDM MTSSGIQSA
//