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Database: UniProt
Entry: A0A3S9T189_9FIRM
LinkDB: A0A3S9T189_9FIRM
Original site: A0A3S9T189_9FIRM 
ID   A0A3S9T189_9FIRM        Unreviewed;       649 AA.
AC   A0A3S9T189;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=BBF96_13165 {ECO:0000313|EMBL:AZR74267.1};
OS   Anoxybacter fermentans.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX   NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR74267.1, ECO:0000313|Proteomes:UP000267250};
RN   [1] {ECO:0000313|EMBL:AZR74267.1, ECO:0000313|Proteomes:UP000267250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY22613 {ECO:0000313|EMBL:AZR74267.1,
RC   ECO:0000313|Proteomes:UP000267250};
RA   Zeng X., Shao Z.;
RT   "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT   Anoxybacter fermentans.";
RL   Submitted (JUL-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; CP016379; AZR74267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9T189; -.
DR   KEGG; aft:BBF96_13165; -.
DR   OrthoDB; 2318150at2; -.
DR   Proteomes; UP000267250; 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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000267250};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}.
FT   DOMAIN          183..364
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   DOMAIN          467..641
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        551
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   649 AA;  71802 MW;  7A3D7AF96C282DF2 CRC64;
     MKDLIQRIFK KSGMTEKDFE LNQLRRQVTV LFSLLSNLYG ADKLVLKAGK LEALNLMRST
     DLAERVVALQ RIVFEDPTID EIPSEKEIPA ILEEIEDGIA DIIARKTVEE KIERQVTEKM
     QEKHNEYIQE IKKQIVRESE GADNPQTLKK YAELEKLEQR GLSRSAMELL RPTSLEEIVG
     QERAIKALMS KVASPYPQHV ILYGPPGVGK TTAARLVLEA AKKMPRTPFD EEAKFVEVDG
     STLRWDPREV TNPLLGSVHD PIYQGARKNL ADIGIPEPKL GLVTEAHGGV LFIDELGEMD
     PMLQNKLLKV MEDKRVYFES SYYDPTDESV PQYIKKLFED GAPADFLLIG ATTRDPSEIN
     PAFRSRAAEV FFEPLTPEHI KKIVNNAAAK LKVKLEVGVD EVISTYTVEG RKAINILADA
     YGLALYELNQ AGKGEEETEI TITKDHIYEV AQISRLTPYV SIKGSDTLEV GKIFGLGVSG
     YLGSVIEIEA IAFKASEKGK GRLRFNETAG SMAKDSVFNA ASVVRKLTGK DIADYDIHVN
     VVGGGRIDGP SAGVAIVLAI ISAIENRPIR QDIAVTGEIS IQGRVKPVGG VFEKIYGAQR
     AGIRQVFVPK DNANDIPKDC KGIEITVVDR VEEIIDLVMP PLKKKAKVS
//
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