ID A0A167EDT0_9BACL Unreviewed; 578 AA.
AC A0A167EDT0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=PNBC_08720 {ECO:0000313|EMBL:OAB75436.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB75436.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB75436.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB75436.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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}.
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:OAB75436.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSFN01000010; OAB75436.1; -; Genomic_DNA.
DR RefSeq; WP_068657215.1; NZ_LSFN01000010.1.
DR AlphaFoldDB; A0A167EDT0; -.
DR STRING; 1763538.LPB68_06675; -.
DR KEGG; pcx:LPB68_06675; -.
DR OrthoDB; 2318150at2; -.
DR Proteomes; UP000077134; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 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:UP000077134};
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..536
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 578 AA; 62391 MW; D568663703CF5B11 CRC64;
MNLSMIFMLI QLFFGVVIGI YFWNLLRGQK TNRTAVDRES RKELDKLRKL RSISLTKPLS
EKTRPQTIHD IVGQKDGLRA LKAALCSDNP QHVIVYGPPG VGKTAAARVV LQEAKKNPAS
PFKNDAKFTE IDATTARFDE RGIADPLIGS VHDPIYQGAG SMGVAGIPQP KPGAVTKAHG
GILFIDEIGE LHSIQLNKLL KVLEDRKVLL ESAYYNSEDT NTPAYIHDIF QNGLPADFRL
VGATTRSPHE IPPALRSRCM EIFFRPLLPE EIGKIAEDAI QKLGLQPCPE AVEVVKQYAT
NGREAVNIIQ LGVGLALTEK RDTLEATDVE WVANSSQLQP RPDRKIPTHP QVGIVNGLAV
YGTNIGTLLE IEVSASTSVK GQGKINITGV VEEEEIGGGT RTIRRKSMAK GSVENVLTVL
RLMGLSACDY DLHINFPGGT PIDGPSAGIA MATAIVSAVK NIPIDHRIAM TGELSIHGKV
KPIGGVIAKV EAAFQAGATT VIIPKDNWQT LFANLNGLQV IPVETIQEVF QNVFGKELVN
HLEEALLPNI AGIYSGTSSS VLQAKSITPG KVTDSGSF
//
