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
//