ID B8D1C4_HALOH Unreviewed; 639 AA.
AC B8D1C4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN OrderedLocusNames=Hore_23310 {ECO:0000313|EMBL:ACL71076.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL71076.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL71076.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL71076.1; -; Genomic_DNA.
DR RefSeq; WP_015924044.1; NC_011899.1.
DR AlphaFoldDB; B8D1C4; -.
DR STRING; 373903.Hore_23310; -.
DR MEROPS; S16.005; -.
DR KEGG; hor:Hore_23310; -.
DR eggNOG; COG1067; Bacteria.
DR eggNOG; COG1474; Bacteria.
DR HOGENOM; CLU_020014_0_0_9; -.
DR OrthoDB; 2318150at2; -.
DR Proteomes; UP000000719; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 177..358
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 457..630
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 541
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 584
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 639 AA; 71549 MW; 00E92AC1ED187113 CRC64;
MSFLDGLFSK DDNKIKKADK KEKELKVLYK KANDYYGKEQ FILKAGKVNA LDLISSSKLF
DKLTALERII YEDPTIQVGK GNFEERILKL EDKIADMLAE RSVEKDIEEQ IAERMEKRQR
EYIKEIKKEI VNDDPPDNPE TLRRLARLEK LDARSLNKSV IDLVRPKSLD EIVGQQRALK
ALVSKIASPY PQHVILYGPP GVGKTTAARL ALEEAKKRQN TPFYGDSKFV EVDGATLRWD
PREVTNPLLG SVHDPIYQGA KKVLAEGGVP EPKTGLVTEA HAGILFIDEI GELDPMLQNK
LLKVMEDKRV KFESSYYDKN DENIPLYIKK LFEEGAPADF ILIGATTRSP SKINPAFRSR
CAEVFFNPLS REDIQQIVIN AVKKLTVKIE DEIPEIISEY TTEGRTAINL LIDAYSLVLY
ENEGADEQEL IITRDKLFEA IQNRRMIPHN KIKSSEKSEI GKVFGLGVNG YLGTVIEIEA
VAFTAEEKGN GKLRFNETAG KMAKDSLFNA AAVIRKITGK KMKDYDLHVN IVGGGNVDGP
SAGIAMLLAL ISAIEEVPLK QDIAVTGEVS IRGNIKPVSG IREKIYAAEQ AGMREVLVPA
ENMIDIQEDW DIKVTPISTV EEALKRVLID QDQLKLSII
//
