UniProt: A0A061PD02

Database: UniProt
Entry: A0A061PD02_9BACL

LinkDB:  A0A061PD02_9BACL 
Original site:  A0A061PD02_9BACL

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (27)   

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ID   A0A061PD02_9BACL        Unreviewed;       557 AA.
AC   A0A061PD02;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=JCM19039_2363 {ECO:0000313|EMBL:GAK12580.1};
OS   Geomicrobium sp. JCM 19039.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX   NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK12580.1, ECO:0000313|Proteomes:UP000027177};
RN   [1] {ECO:0000313|EMBL:GAK12580.1, ECO:0000313|Proteomes:UP000027177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK12580.1,
RC   ECO:0000313|Proteomes:UP000027177};
RA   Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA   Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT   JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL   Genome Announc. 2:e00622-14(2014).
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:GAK12580.1}.
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DR   EMBL; BAXB01000009; GAK12580.1; -; Genomic_DNA.
DR   RefSeq; WP_042426939.1; NZ_BAXB01000009.1.
DR   AlphaFoldDB; A0A061PD02; -.
DR   OrthoDB; 2318150at2; -.
DR   Proteomes; UP000027177; 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; 2.
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:UP000027177};
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   557 AA;  60965 MW;  D1C91F2CBBBDB5DA CRC64;
     MNWTSIIMLV QVFFGIVIGL YFWNLLKNQR TQKVSVDRES RKEMVQLQKL RSVSLNEPLS
     EKVRPESLDD IIGQDEGILS LEAALCGPNP QHVIIYGPPG VGKTAAARLV MNKAKSNEHS
     PFLQEAPFIE LDGTTARFDE RGIADPLIGS VHDPIYQGAG SMGQAGIPQP KPGAITKAHG
     GMLFIDEIGE LHSIQMNKML KVLEDRKVFL ESAYYSEENM NIPRHIHDIF QNGLPADFRL
     IGATTRTPDE IPPAIRSRCL EVFFRPLKQK ELARVAEKSA KRLEMSIHPE GLETIASYVS
     NGREAVNTIQ IAAGLATSEN RNEIGVSDIE WVVHASRLTR RPEKVIHQSP AVGRVNGLAV
     YGPDLGMLLE IEATARKTSE GKGMLTVTGI AEEENAGNQM RSIRRKSMAR SSVDNVMTVL
     RRLQVPVDHY DIHVNFPGGT PIDGPSAGAA IATAIYSAIT NKKVKNDVAM TGELSIWGTI
     KPVGGVPAKV AAALEAGACK AYIPVDNDET VLHRHVGIEV IPLSSLDELF LHVLSEESVL
     MDTTMDHPMN HNQSSSI
//

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