ID I0HYZ3_CALAS Unreviewed; 819 AA.
AC I0HYZ3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, 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 OrderedLocusNames=CLDAP_01910 {ECO:0000313|EMBL:BAL98230.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL98230.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAL98230.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) 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; AP012337; BAL98230.1; -; Genomic_DNA.
DR RefSeq; WP_014431472.1; NC_017079.1.
DR AlphaFoldDB; I0HYZ3; -.
DR STRING; 926550.CLDAP_01910; -.
DR KEGG; cap:CLDAP_01910; -.
DR PATRIC; fig|926550.5.peg.204; -.
DR eggNOG; COG1067; Bacteria.
DR HOGENOM; CLU_014785_0_1_0; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000007880; Chromosome.
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; IPR008144; Guanylate_kin-like_dom.
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; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000007880};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 55..265
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 569..764
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 793..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..247
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 659
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 702
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 819 AA; 91311 MW; 6D55F79CA99C2B00 CRC64;
MSPISPLPPE VLRRRCNPEE FPFDTTEELD GAVGLIGQER PVSALRFGVK MRRQGYNIYA
LGPSGLGKHT LVRRIIEERA AQEPPPSDWC YVNNFSQPYR PRILRLPQGR GRQLKRDMAR
LVEDMQTALS AAFESEEYQA RRRAIESAFQ DRQQATLMQL QEQARQRGLT LLRTPAGLAF
APLKGDEVLT PDEFEKLPEE EQKRIRADVE VMQEELQKVI AQAPRWEREL RNQIRALNQE
IASIVLNDLI AELATSYADM PEVLEYFQEV RRDVQEHLSD FLMAGEKQRQ ASDGENPMAL
VDGASPLRRY QVNLLVDSTD VKGAPVIYES NPTYTNLTGR IEQMAQMGAL VTDFMLIKPG
ALHRANGGYL ILDALKVLSN AYAWEGLKRA LEFGEVRIES VLQILSLTST ISLEPEPMPL
DVKVVLLGDR LLYYLLSQYD PDFSELFKVA ADFADEVERT PEMHLAYAQL ISSIVRKESL
RPLDRYAVGA VIDHAARLVS DSERLTAQIQ AIVDLLQEAN YWAAEANATV ISAEHVQQAI
DAQIFRLDRV ARLIQSEILR RTIHIDTTGA VIGQINGLSV LQLGNFTFGQ PSRITATVRM
GRGDVVNIER EVNLSGPIHS KGVLILASFL NARYATEQPL ALSASIVFEQ SYSGVEGDSA
SSTELYALLS AIGRIPLKQS LAVTGSVDQY GRVQAIGGVN EKIEGFFDLC KARGLTGDQG
VLIPETNVKN LMLRNDVVEA VAAGKFHIYP VSHIDEGIEL LTGVPAGVPN KQGKYPKGTV
NRAVVDRLEH MARKRRALES KEQAQKETKS NDKETPKLE
//
