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Database: UniProt
Entry: A0A081G1Q8_9GAMM
LinkDB: A0A081G1Q8_9GAMM
Original site: A0A081G1Q8_9GAMM 
ID   A0A081G1Q8_9GAMM        Unreviewed;       799 AA.
AC   A0A081G1Q8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=ADIMK_1166 {ECO:0000313|EMBL:KEA64713.1};
OS   Marinobacterium lacunae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA64713.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA64713.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA64713.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) 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:KEA64713.1}.
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DR   EMBL; JMQN01000015; KEA64713.1; -; Genomic_DNA.
DR   RefSeq; WP_036184869.1; NZ_JMQN01000015.1.
DR   AlphaFoldDB; A0A081G1Q8; -.
DR   STRING; 1232683.ADIMK_1166; -.
DR   PATRIC; fig|1232683.4.peg.1156; -.
DR   eggNOG; COG1067; Bacteria.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000028252; 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: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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000313|EMBL:KEA64713.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000028252};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          564..759
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          201..235
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        654
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        697
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   799 AA;  88976 MW;  2FD555E2A6C7EA72 CRC64;
     MALKPLDSDK LYHRCDLSDF GFTSTNDLTP DLSALGQQRA MDALQFAVGM HHDGYNLFVS
     GSTGVGRREL VSRMINERAK QGEAPQDWVY VHNFERAHEP CMLCLPKGAG QGLRQDMQQL
     IERLLIQIPA TFKSDEYRNR VQEISDEFEQ REESQFQALG EKAHEEQITL MRTPSGYTLG
     PLREGKLMTP DQFKALPEAE QTRIKAALEQ LNAELTALVR ELPKLQQEHR EAIRALDDDI
     THSVIDPALS GLRQKYGTES ALLEFLDQVH QDMIENVDDF FAQDKDENAK TPLHKLARSD
     TFRRYRINVL VSHDHNGGSP VVVEDIPSYQ NLVGRIEYQA HFGTLSTDFS LIQPGALHRA
     NGGYLIVDAQ KLLSYPFAWE GLKRALRNRE IRIDPLEKMY GISGTRSLEA EPMPLKLKVI
     LIGERRLYYL LKAYDPEFST LFKVYADFNE QLDRSRGNLE GYLGLITQLV QEEGLAPFAL
     SGIERVIEQS SRRVDDSTKL SLNRGQLIDL LREASYCATR AGSSQVKSEH VSQALKMART
     RSAQYSELMQ EQIERGTIMV ATEGSAVGQA NGLSVFQLGD QRFGKPARIS ATARLGGGKV
     IDIERETELG GPIHTKGVMI LANCIGARYA RNSPLSLHAS LVFEQSYGMV DGDSASALEL
     CVLLSAISGL PIKQSLAVTG SINQRGEIQA IGGVNEKIEG FFELCKNRGL TGDQGVVIPA
     TNVDHLILDQ AVVQACEKGE FHIYAVKELD ELISLLFDRK PGKADEDGRY PPASVNGCVQ
     QQLLDWTEQA RKLSGKSDN
//
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