ID A0A0N6ZX18_9MICO Unreviewed; 369 AA.
AC A0A0N6ZX18;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=NI26_04325 {ECO:0000313|EMBL:AIV39654.1};
OS Curtobacterium sp. MR_MD2014.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV39654.1, ECO:0000313|Proteomes:UP000069933};
RN [1] {ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K.;
RT "Isolation and characterization of species affiliated with family
RT Actinomycetaceae.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIV39654.1, ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV39654.1,
RC ECO:0000313|Proteomes:UP000069933};
RX PubMed=26722011;
RA Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K., Dawson S.C.;
RT "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT from Topsoil in Woods Hole, Massachusetts.";
RL Genome Announc. 3:0-0(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; CP009755; AIV39654.1; -; Genomic_DNA.
DR RefSeq; WP_066652893.1; NZ_CP009755.1.
DR AlphaFoldDB; A0A0N6ZX18; -.
DR STRING; 1561023.NI26_04325; -.
DR KEGG; cum:NI26_04325; -.
DR PATRIC; fig|1561023.3.peg.909; -.
DR Proteomes; UP000069933; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.30.42.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Reference proteome {ECO:0000313|Proteomes:UP000069933};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..355
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 369 AA; 38449 MW; CA87FA3825DA6EC0 CRC64;
MTLFAPAPRR RSRARTVGWA FVIGAVVLGL LASFLPSPYL IEVPGPVYNT IGTQRQGQGK
DAKDVELIQI DGAETYPTGG ALDMLTVGIQ GDATNRPSWT NVIRALFSRS EAVIPASAVY
PEGTTTEQVN QQDEADMRSS QQSAVAAALI HQGHDLPTEL RVGTVQEGSA ADGTIREGDV
ITAFDGEQLT ENVDAGSLRA AVAEHGTSSP ATVTLLRDGK REQVEVTPRE EQGTPLLGVG
VTERYDFPFD VKIALQDVGG PSAGMMFALG IIDELTPGEL NGGKHVAGTG TITADGEVGP
IGGIRQKLYG AKDAGATVFL APADNCDEVV GHVPDGLDVY KVATLDQAVT DLETIAAGKS
TAGLARCGS
//
