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Database: UniProt
Entry: D1Y319_9BACT
LinkDB: D1Y319_9BACT
Original site: D1Y319_9BACT 
ID   D1Y319_9BACT            Unreviewed;       813 AA.
AC   D1Y319;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=HMPREF7215_0309 {ECO:0000313|EMBL:EFB91218.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB91218.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB91218.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB91218.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) 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:EFB91218.1}.
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DR   EMBL; ADFP01000047; EFB91218.1; -; Genomic_DNA.
DR   RefSeq; WP_009164282.1; NZ_ADFP01000047.1.
DR   AlphaFoldDB; D1Y319; -.
DR   STRING; 352165.HMPREF7215_0309; -.
DR   eggNOG; COG1067; Bacteria.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000006462; 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; 1.
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; 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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          566..761
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          793..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        656
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   813 AA;  91331 MW;  138266262203B5F7 CRC64;
     MKIRARKLTA AQVRRKTDPK VLRCSSSAEL EGLTHFIGQE RAVKSIDFGL AVKSTGYNVF
     IVGPQGSGRT SYALKSVREK AARLPAPNDW IYVNNFDEPA TPLAIDLPAG QAKKAEEDFD
     KLIEELKSVI SGAFEKSSYE DAKAQEISSF QDQISKMMNH VREEAEKDGF LVKRTPQGFV
     NIPLKIVKNG KGKKEFKELQ TDEFEALPRK EQKRLKSVSD ALTSKTLEVL RQIREKERAL
     KAKLSDMEAE ICRTAIGPYL DEIREKYGQT KKFAQWIDSL ERQIVANYAL FIAAARDESG
     EVDFTPYRIN VFVGNDPKGG APAVWETNPT FYNIAGKMEY ESRQGYYYTD FTRIVSGALH
     RANGGYLILD AEELLRNFMS YDLLKRVLRS GLLTVENLSD QYSVMPITTP RPEAIPIKTK
     VILVGSYYIY YLLREYDPDF PKFFKTVAEF DCEMPRTPEN EWDMARFVKT TAEQDGCLPF
     NKKALAELIE WASRLADDQN KLSTQFNRLK EYVVESSAWA LSEGAKSVDR KHVLRAIQEK
     RYRSSQTEEK IRAAFAEDII RIDTDGAVVG QINGLAVVSF AEVSFGHPAR ITANTFMGQE
     GVINIEREIL MAGPIHNKGL LTLSSYLGRV YAQDMPLTLS ARLSFEQNYG GIDGDSASST
     ELYCLLSSLA DVPIAQNIAV TGSVDQFGNI QPIGGVNEKI EGFFSYCLAR GLTGSQGVLI
     PWQNERHLML NHDVVEAIRR KQFHIWSVKT IDEGIELLTG RPAGKRRADG TYPEDSIHGR
     AMAKLKRWIE KSAALSRGQK GNAPSALSRE RKQ
//
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