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Database: UniProt
Entry: A0A075NZ51_9ALTE
LinkDB: A0A075NZ51_9ALTE
Original site: A0A075NZ51_9ALTE 
ID   A0A075NZ51_9ALTE        Unreviewed;       798 AA.
AC   A0A075NZ51;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=EP13_09175 {ECO:0000313|EMBL:AIF98836.1};
OS   Alteromonas australica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF98836.1, ECO:0000313|Proteomes:UP000056090};
RN   [1] {ECO:0000313|EMBL:AIF98836.1, ECO:0000313|Proteomes:UP000056090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 17 {ECO:0000313|EMBL:AIF98836.1,
RC   ECO:0000313|Proteomes:UP000056090};
RA   Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT   "Genomes of Alteromonas australica, a world apart.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP008849; AIF98836.1; -; Genomic_DNA.
DR   RefSeq; WP_044056990.1; NZ_CP008849.1.
DR   AlphaFoldDB; A0A075NZ51; -.
DR   GeneID; 78255083; -.
DR   KEGG; aal:EP13_09175; -.
DR   eggNOG; COG1067; Bacteria.
DR   Proteomes; UP000056090; 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; 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:UP000056090};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          566..761
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        656
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   798 AA;  88805 MW;  EB860684AC6D141A CRC64;
     MSGEIKHTSL TPSSLTPTIN RKAINSALKD DEALHATFIG QERAREALTF GLGINAKGYN
     LYVMGEPATG RFTLVRDYIA RQVANLNAPD DWVYINNFAE EREPVALKFP TGGGKAFHKD
     ISQLIDDVLD TFPVAFDNPG YQRKRANISR EFDKKYDEAI AALERYAQAN DVALYEENGE
     ISFSPIVEGK PLTDTEFAAL NESQRSHFYA LIDDLENRLS ESLLSLPSWK RENSEQLRAL
     DKQTAEQGIK PLLKVLEHKY SAELGILKYL KQLKTALVNA ILLIVQEERK DEKSDEFDQR
     VFLEEQFLPN VLVANNVGDT APVIYEPNPT YQNLFGKIEY TNIHGGVFTN YRMIRPGALH
     RANGGYLLLD VDQLIEQPYV WETLKLAVKL GRLKMDLPQQ DVGMVNAITL HPQPIDLNIK
     IVLLGSRDLY YTLQDYDDEF DELFRVLVDF DLEIQVSRQA LFDFVGKVRK HLAQLNIQHV
     TANAMCRLVE YSLRMAEHQQ KLSAHFSEVI ELVNEAHFFC MKSGSDTLEL HHLKTALAAK
     KRRTGRVSQT LLNDIKEGHV LIATEGKAIG KVNGLTVLDI GDTAFGTPAR ITSTVFAGAS
     GVVDIEREVE LGQPIHSKGV MLLTGYLGNK YAQHFPLTLS ANIALEQSYG HIDGDSASLG
     ELVALISALT EIPCLQTLAI TGSINQYGEV QAVGGVNEKI EGYFDLCQHR GLTGTQGVII
     PKSNAINLVL DSTVIDAVKK GLFHIYTVET VDDALSILME QEAGVLSSRS RYPKNTINYH
     AVNRLYNIAL IVNGGDGE
//
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