ID A0A286G8Z4_9PROT Unreviewed; 811 AA.
AC A0A286G8Z4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=SAMN05421508_102197 {ECO:0000313|EMBL:SOD91965.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD91965.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD91965.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD91965.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCNJ01000002; SOD91965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286G8Z4; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000219621; Unassembled WGS sequence.
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; 2.
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:UP000219621};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 568..763
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 811 AA; 89891 MW; A5B7F208FE7D046C CRC64;
MPLDPLPADR LHTPCREADL PFETTAELPD QEDTVGQERA VEAVRFGIGI RADGYNIFAA
GPQGTGKSSL VRQFIGRAAA AQPRPDDWCY VHNFDDPQRP RALRLPAGRG RAFQRAMERL
VEELQAAIPA AFEADDYRAR RQAIEDEFKE RQERTFGEVQ TKARARGVAL VRTPVALALA
PLKDGEVLSP DEFEKLSEDE RADRKQAMEE LQEDLQTRMR EIPKWEKEQR ERVRELDRDV
TEYAVGHLID DLRADYEDCP AVLAHLDTVR KNLVERVDQF LPESEELRQL PPQIRKQLGG
NREETHEQYK VNVVIGRHEN GGAPVVEEDH PSQPNLVGRI EHQQRYGALV TNFTLIRPGA
LHRANGGYLV LDARKLLMQP FAYEDLKRAL RTREIRIEAP GASFGIFTTT SLEPEPIPLD
VKVVLIGEPM VYYLLSHHDP EFRELFKVQA DFDYRMHRRD DTTLALARLV GTMARRDGLR
PLDRSAVARV IDHAARLADD SERLTTHMGS VADLVREADF WAGERGAEVV SRRDVQQAID
AKTYRTDRVR EHIQEEFARG TLMVDTDGEK AGQINGLAVL QLGTFAFGRP SRITCRVRMG
RGELVDIERE VGTGGELHTK GVLILSGFLA ARFGQDGPLS VSASLVFEQS YGLIDGDSAS
CAELYALLSA LADVPIRQGF AVTGSVNQFG EVQPIGGVNE KIEGFFDVCA ARGLTGDQGV
LIPASNVKNL MLRPDVVEAA AAGRFHIHAV STVDEGIEIL TGIPAGAPDD GAGWPTGSIN
RRVAARLAQW RRRALELSAA GSGRNGNGGR G
//