ID A0A366WBD1_9GAMM Unreviewed; 576 AA.
AC A0A366WBD1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=DS885_04475 {ECO:0000313|EMBL:RBW47164.1};
OS Psychromonas sp. B3M02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=2267226 {ECO:0000313|EMBL:RBW47164.1, ECO:0000313|Proteomes:UP000252071};
RN [1] {ECO:0000313|EMBL:RBW47164.1, ECO:0000313|Proteomes:UP000252071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3M02 {ECO:0000313|EMBL:RBW47164.1,
RC ECO:0000313|Proteomes:UP000252071};
RA Enke T.N., Datta M.S., Schwartzman J.A., Cermak N., Schmitz D.A.,
RA Barrere J., Cordero O.X.;
RT "Modular assembly of carbohydrate-degrading microbial communities in the
RT ocean.";
RL Submitted (JUL-2018) 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 -!- 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:RBW47164.1}.
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DR EMBL; QOCB01000032; RBW47164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366WBD1; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000252071; Unassembled WGS sequence.
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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000252071};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 341..538
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 576 AA; 64155 MW; F1CF8229E9628D24 CRC64;
MPSFYLTRAE ILTNNISPVT LDNASSTTQL ELEKTTPLSI SQCTPAFTGY IEQYVAPSEL
AFSPLFTNAT AIIEKYLKLP VPLLLVNSRY WLNAQQVLKE VIPNDLPVDY LLSYNQESLF
GRASLNADDT LHLSQGLLNT FNNGALVLNI SPLLVESNLW FKLKSVLQRG YLLASDAVNA
DKSKQALPDL QSQPINIKLI LVASRAQLEE LIQIDPEYTQ ISSLFCELAS QVPVNQTSIN
TVIHYCQHLA AQLGLTPLND KALQIILNAL SIECQHQQQL LFDLEFIEQT IRYANLFTEN
KRVTEDDLSA YFDEINEAQS LARKYSEQSV IEGQVNLQLT GEKIGQINGL SVVELLGYPC
EFGEVFRISA SDMIGDGEII DVERKVELAG NIHAKSTHIV QGYLNHFFSH ISAFPYSCNL
VFEQSYQESD GDSASLAILL AVSSCYAKCA VKQDVFVTGS LDQHGNVLPI GGINQKIESV
SRLFELGLLT DPVTIVMPKA NMLNLTLNKY SLALIEEGKL LIHAINHCHQ AFPILLNKSF
EQIIKTINCR IELANKEEME ESSIGLFSRL KHSIFH
//
