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Database: UniProt
Entry: F7P0D2_9GAMM
LinkDB: F7P0D2_9GAMM
Original site: F7P0D2_9GAMM 
ID   F7P0D2_9GAMM            Unreviewed;       796 AA.
AC   F7P0D2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=Rhein_3532 {ECO:0000313|EMBL:EGM76470.1};
OS   Rheinheimera sp. A13L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM76470.1, ECO:0000313|Proteomes:UP000004282};
RN   [1] {ECO:0000313|EMBL:EGM76470.1, ECO:0000313|Proteomes:UP000004282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A13L {ECO:0000313|EMBL:EGM76470.1,
RC   ECO:0000313|Proteomes:UP000004282};
RX   PubMed=21742876; DOI=10.1128/JB.05636-11;
RA   Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT   "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5873-5874(2011).
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:EGM76470.1}.
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DR   EMBL; AFHI01000056; EGM76470.1; -; Genomic_DNA.
DR   RefSeq; WP_008900357.1; NZ_AFHI01000056.1.
DR   AlphaFoldDB; F7P0D2; -.
DR   STRING; 506534.Rhein_3532; -.
DR   eggNOG; COG1067; Bacteria.
DR   OrthoDB; 9758568at2; -.
DR   Proteomes; UP000004282; 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; 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   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   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          564..759
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        654
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        697
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   796 AA;  88832 MW;  AC66BAA96C102CBB CRC64;
     MTHNSHKYAL TAEHLGPQLD KNLIQQALDV SGLSSTFIGQ DRAKAALNFA IGMDMPGYNL
     YVMGEPALGR YTLVQDILQQ AASEKATPDD WCYINNFDDE RIPGTLRLVP GEGKVLVKKV
     EALIDELLDT FPAAFDNPGY QRKKKAIHQE FDDKYEAAIA LVERKALEQQ VVLYEENGAV
     SFSPVVDGKA LDDNEFANLS EEKRQFFYDL VSELETILNE QLLELPQWKR ELSENLRALR
     RETIEQAIKP LLKQLEHDYS AELGVLRYLR EMKPALVKAM LELLPEEAES DKLEELDIRG
     IFVGDFVPNV LMHHELMDGA PIIFEPNPSY GNLFGRVEYS SMQGSLYTNY RMIRPGALHK
     ANGGYLVLDA DRLLSQPSLW DALKLALKTG EILIDTLSDH AVTNSTIITP KAIPLSVKIV
     LLGSRDLYYL VQDVDDEFNE LFRVLADFEH YLPFNEQTVR YMSLQIQDQI QQMDMETLSA
     CGLKQLLNFS FRQAEHQRKL SARFAEVLEL VREACFYAAQ HDSAELRAEH VQMALEGKQY
     RTGRISESFL EDIQEGQILI DTDDWAVGKI NGLTVLEIGD TAFGTPARIS TTVFAGSTGV
     VDIEREVELG KSIHSKGVML LTGYLGAKYA QHFPLTLSAN IAMEQSYGLI DGDSASLAEV
     CALISGIADI PITQSLAVTG SINQHGQVQA IGGVNEKIEG FFRLCESRGL TGKQGCIIPA
     SNQLNLVLND EVIKAVEQGQ FHIYVVKGVD EALELLMDMP AGERNSKGQY PKRTINYLAL
     RRLEEIAEIV NGSSDS
//
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