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Database: UniProt
Entry: A0A0M3RE68_9BACI
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ID   A0A0M3RE68_9BACI        Unreviewed;       571 AA.
AC   A0A0M3RE68;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=AM500_08270 {ECO:0000313|EMBL:ALC89766.1};
OS   Bacillus sp. FJAT-18017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC89766.1, ECO:0000313|Proteomes:UP000060713};
RN   [1] {ECO:0000313|EMBL:ALC89766.1, ECO:0000313|Proteomes:UP000060713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC89766.1,
RC   ECO:0000313|Proteomes:UP000060713};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000256|ARBA:ARBA00026070}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; CP012602; ALC89766.1; -; Genomic_DNA.
DR   RefSeq; WP_053598791.1; NZ_CP012602.1.
DR   AlphaFoldDB; A0A0M3RE68; -.
DR   STRING; 1705566.AM500_08270; -.
DR   PATRIC; fig|1705566.3.peg.1780; -.
DR   Proteomes; UP000060713; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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   CDD; cd00009; AAA; 1.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR014251; Spore_LonB.
DR   NCBIfam; TIGR02902; spore_lonB; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF64; LON PROTEASE; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
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.
DR   PROSITE; PS01046; LON_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000060713};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          349..535
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        488
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   571 AA;  61946 MW;  80C756BC3B457480 CRC64;
     MSWMGIALFV QLFFGIIIGL YFWNLLKNQR TQKVTIDKES KKEMEQLRKM RSISLTEPLA
     ERVRPGSFDD IVGQKDGIKA LKAALCGPNP QHVIVYGPPG VGKTAAARLV LEEAKRNQKS
     PFQQSSVFIE LDATTARFDE RGIADPLIGS VHDPIYQGAG AMGQAGIPQP KQGAVTNAHG
     GVLFIDEIGE LHPIQMNKLL KVLEDRKVFL ESAYYHEENP SIPTHIHDIF KNGLPADFRL
     IGATTRTPNE IPPAIRSRCM EVFFRELSQD EIMTVAKKAA DKVEMAINES GLEILSNYAR
     NGREAVNMIQ TAAGLAITQD RKEIKDEDIE WVIHSSQASP RMERKINDLP AIGLVNGLAV
     YGPNSGALLE IEVSVIPAKE KGSINITGIV EEESIGGQGK SIRRKSMARG SIENVITVLR
     TMEVPADEFD IHVNFPGGIP IDGPSAGIAM ATGIYSAIYK IPVDNRIAMT GEISIHGHVK
     PIGGVFAKVV AAKKAGAKTV IVPAENMQSI LNEIDGIEII PVTHFNEVID LALKKDSSNN
     SVPQSGGTHV IAEGDGTVIP AAVQMSKKES V
//
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