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Database: UniProt
Entry: A0A0J1H8Z4_9GAMM
LinkDB: A0A0J1H8Z4_9GAMM
Original site: A0A0J1H8Z4_9GAMM 
ID   A0A0J1H8Z4_9GAMM        Unreviewed;       791 AA.
AC   A0A0J1H8Z4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=ABT57_15330 {ECO:0000313|EMBL:KLV08174.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV08174.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV08174.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV08174.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) 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:KLV08174.1}.
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DR   EMBL; LDOU01000015; KLV08174.1; -; Genomic_DNA.
DR   RefSeq; WP_047886063.1; NZ_PYMI01000004.1.
DR   AlphaFoldDB; A0A0J1H8Z4; -.
DR   PATRIC; fig|320778.3.peg.3335; -.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000035909; 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; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR046844; Lon-like_helical.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
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:SF46; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000035909};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          567..762
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          213..244
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        657
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        700
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   791 AA;  88626 MW;  2D5B7F6280DDA9BD CRC64;
     MTIKTLSSDK LYRVSELHGL PEDCKSTKNL TPLDEIVGQE RAQQAVEFAM SIKEKGYNIY
     AIGRNGLGKR TMVLRYLNRH DPNGSGHPQH DWCYVANFEE SRNPKVLKMP AGRGTQFKKD
     VEKMMTKLVK ALPLAFDNEV YYSRSEKLKN QLDQKQQGAL LALTQEAKEH SISLTVTMAG
     EYQLVALNGE EPHTEESFAQ LSDKEQKVFE DTINALEKKL RSIVRELTEL EEDFSEKMQK
     LNEEIALEVV SHFIHDLLIE YKSLPEVKNY LKAMRKDILE NLDIFLEESE EDVALAYATL
     DKKMPRRYQV NVLVANDTET KFPIVVEESP NYHSIFGYVE NATYKGTIFT DFSLIRSGSL
     HRANGGVLLM DAVKVLERPY VWDGLKRALR SRKLSVSSLE KEVTLSGTIS LDPEPIPLSV
     KIILFGDYQT YQLLQHYDPE FSELFRVTAD FEDEMCRTDE SEAQYAKFIS SIVNDNNMLH
     CDRKAIARII EYSSRQADDQ NKLSLHSADI ANLLRESNYA AKSSNATMIR ANHVEQALHS
     QEKRVSRLKD HVMQTFTNGT TLIDTEGAVV GQINGLSVIS TSDYQFGAPN RITATTSYGE
     GGVFDIERSV DLGGRIHSKG VMILSAYLAS IFGRSSRVPL TTHLTFEQSY GGVDGDSASM
     AELCAIVSAY SQIPLRQDVA ITGSMNQFGQ AQPIGGVNEK IEGFFDVCTI KGRHAAQGVI
     IPQSNAHNLM LRKDVVEAVE KGEFHIWAIS HVTDAIEIMT GKQAGQASLD GTYPVESVLG
     QAQMKLNALR R
//
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