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Database: UniProt
Entry: A0A2Z6DY94_HYDTE
LinkDB: A0A2Z6DY94_HYDTE
Original site: A0A2Z6DY94_HYDTE 
ID   A0A2Z6DY94_HYDTE        Unreviewed;       792 AA.
AC   A0A2Z6DY94;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=HPTL_1230 {ECO:0000313|EMBL:BBD77494.1};
OS   Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila).
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales;
OC   Hydrogenophilaceae; Hydrogenophilus.
OX   NCBI_TaxID=297 {ECO:0000313|EMBL:BBD77494.1, ECO:0000313|Proteomes:UP000262004};
RN   [1] {ECO:0000313|EMBL:BBD77494.1, ECO:0000313|Proteomes:UP000262004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH-1 {ECO:0000313|EMBL:BBD77494.1,
RC   ECO:0000313|Proteomes:UP000262004};
RA   Arai H.;
RT   "Complete genome sequence of Hydrogenophilus thermoluteolus TH-1.";
RL   Submitted (APR-2018) 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; AP018558; BBD77494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6DY94; -.
DR   KEGG; htl:HPTL_1230; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000262004; 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; 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; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000262004};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          557..753
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        648
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        691
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   792 AA;  86810 MW;  76EF3F3551A2EC28 CRC64;
     MTQIATLDPQ SLYRRTQLDT QPVPDSTHRP PFVGQDAALE TLALALADAR RGHVVLMAPP
     GYGRHAIARW TAEQAARKRL SPHDLLYVPR FDDPLRPQLL RLPAGKGREL AAAVERLVQR
     LPELVRGALT ADPHRTRIEA LLKRHQERQQ QALAEIRDGC AGDRLKLLQT DDGWALVPTD
     EHGEPFTPEA YAALPETERK RWEERVARWR DRLAAVLARF PEWDEALADA IDAAERDALA
     PVARHLLHPL REAFADFSEV LAYLDAFEAE LVRGPRPWLA RDGTEVLIDE AVLAHYLVNP
     SVVHEAQAHA PVCLGENISH ATLVGWVESE VVEDERISDH RHIRAGHLAQ AADGFLLVDA
     TALLADSDAW QALKRTLATQ RVEVAPPPAQ TRWGALPLVR PDPIPFAGQV ILIVTPEIYE
     ALRDLDETFT TLFPWVVELE HTVPRTPENE ARYAAVLRQL LADDGDDGPE VSDDAIARAL
     EAAARAAEDQ QRLALTVGRF AGLLREAAAW AQAQGRKVVA RQDVEAAVRA RFARTGSAWR
     ETIAAIADGT HLITTRGNRV GQVNGLVVFE SGEEAYGHPI RITASVRMGG EGEVLDIERE
     SELGGSIHSK GVMILSAFLS GRFGRRRPLA LSATLVMEQS YGFVEGDSAS LAEALALLSA
     IAGVPLEQSI AVTGSINQFG EVQAVGAINE KIEGWYAVCA AAGLDGSHGV ILPAANCRHL
     MLDDAVIAAV RAGRFHLWPV RSVDEAAAVL TGRPIRGPQS LPARVADALA HFARWHDEKG
     ASWRRPWQRR RE
//
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