ID A0A1B1ECE6_VIBNA Unreviewed; 546 AA.
AC A0A1B1ECE6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=BA894_08005 {ECO:0000313|EMBL:ANQ26392.1};
OS Vibrio natriegens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ26392.1, ECO:0000313|Proteomes:UP000092577};
RN [1] {ECO:0000313|EMBL:ANQ26392.1, ECO:0000313|Proteomes:UP000092577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ26392.1,
RC ECO:0000313|Proteomes:UP000092577};
RA Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT "Developing Vibrio natriegens as a novel, fast-growing host for
RT biotechnology.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; CP016351; ANQ26392.1; -; Genomic_DNA.
DR RefSeq; WP_065296849.1; NZ_JAPQMX010000024.1.
DR AlphaFoldDB; A0A1B1ECE6; -.
DR STRING; 691.BA893_08210; -.
DR OrthoDB; 9758568at2; -.
DR Proteomes; UP000092577; Chromosome 1.
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}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 311..508
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 546 AA; 60564 MW; E8ACA8F2FEB50D72 CRC64;
MNQLNWQDVT PSFDEYEALL KSASTLPKKT FVDLQPRMSA TISRFTNIGG LTRILLINCV
DNSIYRGFIS KAVEQSASSP VVTTESLDAK HLFDRYSIAE NGEVTLEQGL IAQADGGYLM
VPANLILANP GYWPSIKAAI QKQPFAAMNM SPTRVAVPAV TSNTYDVKLI VTGDRSQLAE
LEYVDEDFSS GLCMYTEVEE DIHLSQDNLS SYLGYVNWVC AEYNLPSLDK DAYRRLMLAG
MREMEDQHYL PLGVMWHCQL LTLANQHCDS EVIDFKAIDN AIDDKYYRES YLPQRAVYDI
LDGQVIIETT GEQVGQINGL TVIDMAGHPV SYGEPARISC VIHFGDGDVS DVERKAELGG
NLHAKGMMIM QAFLSSALNF DEPLPYAASI VFEQSYSEVD GDSASLAELC CLVSALSECA
VDQQIAVTGA VDQFGRVQAV GGLNEKIEGF YQVCKHQGFT GRQGVILPET NLKHLALHKS
VIESIQNGEF NIWSVSTVDE AIPILMGKPF RGEDDSIIGK IAERIENFER HEHTEGFVQR
IKNWFV
//
