ID A0A1B2M1E0_9GAMM Unreviewed; 881 AA.
AC A0A1B2M1E0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=BFG52_11835 {ECO:0000313|EMBL:AOA58971.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA58971.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA58971.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA58971.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; CP016895; AOA58971.1; -; Genomic_DNA.
DR RefSeq; WP_067556426.1; NZ_CP016895.1.
DR AlphaFoldDB; A0A1B2M1E0; -.
DR STRING; 1789224.BFG52_11835; -.
DR KEGG; ala:BFG52_11835; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000093391; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR046844; Lon-like_helical.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR046843; LonB_AAA-LID.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF20436; LonB_AAA-LID; 1.
DR Pfam; PF20437; LonC_helical; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 601..796
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 691
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 881 AA; 99414 MW; 52ADE2BDCAEE7326 CRC64;
MTQQHEKPHA KLSTLSKPLL DANNNSYPTI FEQSHLQETL EHTRLSAKEL THTPDITQIP
SSTRRLHPLN NFLGQDRAKA SVEAGIALPY SGYNIFAVGT AGLGKRTMIK RLLQQHAKLM
PTPDEWVYVN NFKNPRLPIA LRFPAGQALK FQNQLHQNWH SIIKQLERRF SAETYHNRIE
RIRQETGLEQ QHALVELTHE GELLDLKLVN RNDEHRFVPI QRVEGEIIEL DQEQINALDS
QQRAEIASNI RYMDKKLQRL GLELGNLEDN ARDQVSLLNR DIAKQVVTPR IQQLIEKHKE
VKGLEAYLKA YLQDIIDQVE LILEQEEDDL VAGSFNRIPI RYQANVVVNH KPNSGAPVLF
DDFPTHYNLL GHVEQFTHNG TISTDFTLIR PGALHRANGG FLLLEAEQLL EQPYAWQGLK
RALKSGQLKL SSLEHMLTLT GSISIEPEPI PLQLKVVLLA EPEIYYEILE LEPELGSVFK
IRADFTDTLP RNSSNELAYM QLIADYVQQD KLLPFDRSAL SALLTDSSRQ AEDQSSLSLH
ALTLGDLIRE SHHHAMQTGK KMVTAEQVNT ALKHRQYRLG YLRELYWQDL SRGTQLIETR
GHRLGQINAL SVIHYADVEF GLPSRLTASV YQGGGDILDI ERSVELGGSL HAKGVLLMAS
FLKAHFGRAQ ILHFSAALAF EQSYGQVDGD SATVAELSAL ISAISQLPID QSWAITGSMN
QLGQVQPIGG VNAKIEGFFD ACKLQGLTGQ QGVIIPRQNM QHLMLRPDVI EAVENTKFHI
HAIETIDQAL EILMARPVGQ LDKKGRYSKG SIYAAVMSQL EYWQAIEDGA EIEEVPAKKL
KKKSKKSKKE DKENTEATAD SVELCQHHQP LKKRKKLKKL K
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