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Database: UniProt
Entry: A0A0C4WGX1_9GAMM
LinkDB: A0A0C4WGX1_9GAMM
Original site: A0A0C4WGX1_9GAMM 
ID   A0A0C4WGX1_9GAMM        Unreviewed;       806 AA.
AC   A0A0C4WGX1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=Achr_9560 {ECO:0000313|EMBL:AJE20438.1};
OS   Azotobacter chroococcum NCIMB 8003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20438.1, ECO:0000313|Proteomes:UP000068210};
RN   [1] {ECO:0000313|EMBL:AJE20438.1, ECO:0000313|Proteomes:UP000068210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20438.1,
RC   ECO:0000313|Proteomes:UP000068210};
RX   PubMed=26061173;
RA   Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT   "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT   (ATCC 4412).";
RL   PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE20438.1; -; Genomic_DNA.
DR   RefSeq; WP_039802334.1; NZ_CP010415.1.
DR   AlphaFoldDB; A0A0C4WGX1; -.
DR   STRING; 1328314.Achr_9560; -.
DR   GeneID; 61932262; -.
DR   KEGG; acx:Achr_9560; -.
DR   HOGENOM; CLU_014785_0_1_6; -.
DR   Proteomes; UP000068210; 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:UP000068210};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          563..758
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        653
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   806 AA;  88794 MW;  2221AA9559DAACCB CRC64;
     MPDSVAAGLR LAPDELTRPF DPAQFAFAST DELEPFRGVL GQERAVEALQ FGVAMPRPGY
     NVYVMGEPGT GRFSYVRRYL QTEAKRLDTP PDWVYVNHFE EPREPRSLQL VAGSASEFIA
     DINLLIDNLL ATFPAVFETP TYQQKKSAID RGFNQRYDRA LDSIERQALD KGIALYRDSA
     NIAFTPMKDG KTLDEGEFAQ LPEAERERFH EDIGYLEERL NEELSSLPQW KRESSNQLRQ
     LNEETITLAL QPLLAPLSEK YAESAGVCAY LQAMQVNLLR TVVEQLGDEN VTDAQRRALV
     VEQYCPSLVV GHHCQGGAPV VFEPHPTYDN LFGRIEYGTD QGALYTSYRQ LRPGALHRAN
     GGFLILEAER LLGEPFVWDA LKRALHSRQL KMESPLAELG RLATVTLTPQ VIPLQVKVVI
     VGSRQLYYAL QEVDPDFQEM FRVLVDFDEE IPLADDSLEQ FAQLLKTRTS EEGMAPLSGP
     AVARLATYSA RLAEHQGRLS ARIGDLFQLV SEADFVRQLA GEALTDVGHI ERALKAKETR
     TGRVSARILD DMLAGIILID TQGAAIGKCN GLTVLEIGDS VFGVPARISA TVYPGGSGIV
     DIEREVNLGQ PIHSKGVMIL TGYLGSRYAQ EFPLEISASI ALEQSYGYVD GDSASLGEVC
     TLISALSRTP LKQCFAITGS INQFGEVQAV GGVNEKIEGF FRLCEARGLT GEQGVIIPRA
     NVTNLMLDER VLQAVRAGRF HVYAVRQVDE ALSLLLGEPA GAADEQGCFP TGSVNARVVE
     RLREIAEMGM EEDSGKPKEP QIGVQE
//
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