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Database: UniProt
Entry: S6HQP6_9GAMM
LinkDB: S6HQP6_9GAMM
Original site: S6HQP6_9GAMM 
ID   S6HQP6_9GAMM            Unreviewed;       793 AA.
AC   S6HQP6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=OFPII_12970 {ECO:0000313|EMBL:EPJ47410.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ47410.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ47410.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPJ47410.1}.
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DR   EMBL; ASZJ01000066; EPJ47410.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HQP6; -.
DR   PATRIC; fig|1330036.3.peg.1233; -.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
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; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF49; LON PROTEASE HOMOLOG-RELATED; 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:UP000014822};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          560..756
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        650
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        693
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   793 AA;  87345 MW;  90F09318B9AB38E9 CRC64;
     MSLTPLTAEQ LYKKCDPNLF DFTDTSTVKK FDGCFGQNRA LQAMTFGVGM RRPGYNFFVM
     GNPHTGRSSF TMDMLNSVAS QEVTPSDWIY INNFEDGRSA IAISLPAGRA AKLKADHQIL
     LEAISTELPG AFESPDFQRK KSQIEKQFNA LYDTALDDVE QSARGLSVAM YRDAGNLGFA
     PVSDGKVLDE AEFLLLDEKI RQSINQNIAD LEDLLSESLT ALPVWRREAA EQMKHLEKTT
     TIKAVQPLLA KLQKAYKKHP KLTAYYLKML VHLADHTEDF LNDEKSGELL TDTVRRALLQ
     EWYSINLFVD NSNTKGTPVI YDPHPIYENL FGRVEVANDL SVLATSYLRI RSGTLHKANG
     GYLVIDAEKL LEMPQVYAAL KRALKAQEVR IEAPSDVAGS AISQTPLPVD LQVKVALVGA
     RSTYYLLQDF DADFEKTFRV VVDFDEVVPR TADSIRSYAR LIKTLAAQEG LAAFTRDAVV
     RLIEHSSRSA DDTSMLSSHI GDIVDLLCEA DYKRNQAGDS LVSSKHINLA LHAQQARTGR
     LSERIIDNIV NEVILIDTQG EKVGKCNGLT ILQVGDTSFG TPARITATVY PGKQGILDIE
     REAELGQSIH SKGILILSGY LGFKYAKGFA IQISANIAME QSYGTVDGDS ASLAEVCALI
     SSLTKIPISQ SFAVTGSINQ YGEVQAIGGV NEKIEGFFEV CKKREFVGGP QGVIVPVANI
     RNMMLKQEVI KAVERGHFFI YAVDSVDQCL SLLMGIAAGV LSTDDCYDQH SINAIAVDCF
     KQLSMIKADR TTY
//
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