ID U5RXM1_9CLOT Unreviewed; 631 AA.
AC U5RXM1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lonC {ECO:0000313|EMBL:AGY76314.1};
GN ORFNames=CAETHG_2097 {ECO:0000313|EMBL:AGY76314.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY76314.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY76314.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY76314.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY76314.1; -; Genomic_DNA.
DR RefSeq; WP_013240835.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RXM1; -.
DR MEROPS; S16.005; -.
DR KEGG; cah:CAETHG_2097; -.
DR PATRIC; fig|1341692.11.peg.2122; -.
DR HOGENOM; CLU_020014_0_0_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR014252; Spore_LonC.
DR NCBIfam; TIGR02903; spore_lon_C; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF64; LON PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
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.
DR PROSITE; PS01046; LON_SER; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 178..376
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 459..631
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 631 AA; 70568 MW; 358A0055B5D06FDA CRC64;
MKLQFVDGLN RELNDSIPIN TQVKVLYDLL KKIMDKGTVN ARVVRYNLKG YMNSENLFER
IYALNKIVSD GKGLTEIPDE SNVYDALEST NNWIAETLAE RYVRTKIEKE VEKNLTEHQD
KYMDEVRLSI IKKRKGPENA KTLKKYAQLE VLDSKGLSKN IQKLLRPETF DEIIGQERAI
KSILSKIASP YPQHIILYGP PGVGKTTAAR IALEEAKKLK FTPFRKDAKF VEVDGSTLRW
DPREITNPLL GSVHDPIYQG TKRDLAEVGV PEPKPGLVTE AHGGVLFIDE IGELDEMLQN
KLLKVLEDKR VEFSSSYYDP DDENIPKYIK YLFEKGAPAD FLLIGATTRE PSEINPALRS
RCTEVYFEPL SVKDIQRIVE DAAEKLNIEI ESGVSELISK YTIEGRKAIN ILSDVYGYVL
YNNGISDLND KVKISVEDLK KVISISRFVP FEEVPSKSTY EIGHIYGLGV SGYIGSTIEI
EAVTFEAKEK GKGIVRFNDT AGSMAKDSVF NAASVIRKIT DKDMSDYDIH VNVIGGGRID
GPSAGAAITV CIISALLQKP LRQDVAVTGE ISLRGKIKPV GGIFEKAYGA RRKGIKTMLL
PVENLKEVPT DIKDIEIKAV SNIEELIELI F
//
