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Database: UniProt
Entry: Q97CY0_CLOAB
LinkDB: Q97CY0_CLOAB
Original site: Q97CY0_CLOAB 
ID   Q97CY0_CLOAB            Unreviewed;       634 AA.
AC   Q97CY0;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   Name=lonB {ECO:0000313|EMBL:AAK81636.1};
GN   OrderedLocusNames=CA_C3716 {ECO:0000313|EMBL:AAK81636.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK81636.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK81636.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81636.1; -; Genomic_DNA.
DR   PIR; A97356; A97356.
DR   RefSeq; NP_350296.1; NC_003030.1.
DR   RefSeq; WP_010966976.1; NC_003030.1.
DR   AlphaFoldDB; Q97CY0; -.
DR   STRING; 272562.CA_C3716; -.
DR   MEROPS; S16.005; -.
DR   GeneID; 45000212; -.
DR   KEGG; cac:CA_C3716; -.
DR   PATRIC; fig|272562.8.peg.3905; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_020014_0_0_9; -.
DR   OrthoDB; 2318150at2; -.
DR   Proteomes; UP000000814; 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; 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; 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:UP000000814};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}.
FT   DOMAIN          180..363
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   DOMAIN          460..634
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   634 AA;  70693 MW;  21301B8909273E9F CRC64;
     MKLQSDSEEI RKEDSKTIPL DVQVNALYDT VKNILDDKTI RARIIKYKLN KYLSSKDSAK
     KIYAVNKIIS EGKGIAVIPT NEEETYEAVE DTTNWIVENV AKRYIQNEIE NEVEDALVKR
     QNKYLEEVRL GIIRKKKGPE NKSTLKKYDK LKKLEKIKLS KSIQSLLRPQ TFSEIVGQER
     AIKALVSKLA SPYPQHIILY GPPGVGKTTA ARIALEEVKK LKYTPFKKDA NFVEVDGATL
     RWDPREITNP LLGSVHDPIY QGSKRDLAET GVPEPKSGLV TDAHGGVLFI DEIGELDVML
     QNKLLKVLED KKVEFSSSYY DPDDENVPKY IKYFFEKGAP ADFVLIGATT KDPSEINSAL
     RSRCTEVYFE PLSSSDIMDI IDNAADKLNV LLEDGVKELI SRYTIQGRRA INILADVYGY
     VLYSQGLEPS DKVEIKVKDV ETIVGISRLT PYEKNIFDAE YEVGHVFGLG VSGFMGSTIE
     IEAEAFEAKQ KGKGTIRFNE TAGSMAKDSV FNAASVIRKL TDKDIKDYDI HVNVIGGGKI
     DGPSAGSAIT ICILSAILNK EVRQDVAMTG EISLRGKIKP VGGVFEKIYG ARRRGIKLVT
     VPEDNAKDVP QGLKDIEVKS VTNIEELINI VFKK
//
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