ID   BRXL_ECOHS              Reviewed;         694 AA.
AC   P0DUG1; A0A7M3S2P6;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Lon-like protease BrxL {ECO:0000303|PubMed:30418590};
DE   AltName: Full=BREX protein BrxL {ECO:0000303|PubMed:30418590};
GN   Name=brxL {ECO:0000303|PubMed:30418590}; OrderedLocusNames=EcHS_A0341;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=HS;
RX   PubMed=30418590; DOI=10.1093/nar/gky1125;
RA   Gordeeva J., Morozova N., Sierro N., Isaev A., Sinkunas T., Tsvetkova K.,
RA   Matlashov M., Truncaite L., Morgan R.D., Ivanov N.V., Siksnys V., Zeng L.,
RA   Severinov K.;
RT   "BREX system of Escherichia coli distinguishes self from non-self by
RT   methylation of a specific DNA site.";
RL   Nucleic Acids Res. 47:253-265(2019).
CC   -!- FUNCTION: BREX systems (bacteriophage exclusion) provide immunity
CC       against bacteriophage. Part of a type 1 BREX system which protects
CC       against dsDNA phage. This system allows phage adsorption but prevents
CC       phage DNA replication, without degradation of the phage DNA.
CC       Methylation of bacterial DNA by PglX guides self/non-self
CC       discrimination. When the brxA-brxB-brxC-pglX-pglZ-brxL genes are
CC       transformed into a susceptible E.coli strain (BW25113) they confer very
CC       high resistance to infection by bacteriophage VR7 and VpaE1, about 100-
CC       fold protection against lambda, T5 and T7 and no protection against RNA
CC       phage Qbeta, ssDNA phage M13 or dSDNA phage T4 and VR5. Glycosylated
CC       phage DNA is not susceptible to BREX. The BREX system does not confer
CC       resistance to lysogenic lambda phage, i.e. prophage that are integrated
CC       into the chromosomal DNA and then induced to form phage. Expression of
CC       this protein alone is toxic. {ECO:0000269|PubMed:30418590}.
CC   -!- INDUCTION: Transcribed at similar levels in lag and exponential phase,
CC       rises in stationary phase. {ECO:0000269|PubMed:30418590}.
CC   -!- DISRUPTION PHENOTYPE: Methylation of 5'-GGTAAG-3' in chromosomal DNA,
CC       however BREX no longer confers phage resistance.
CC       {ECO:0000269|PubMed:30418590}.
CC   -!- SIMILARITY: Belongs to the BrxL family. {ECO:0000305}.
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DR   EMBL; CP000802; ABV04729.1; -; Genomic_DNA.
DR   RefSeq; WP_001193073.1; NC_009800.1.
DR   AlphaFoldDB; P0DUG1; -.
DR   SMR; P0DUG1; -.
DR   KEGG; ecx:EcHS_A0341; -.
DR   OMA; FRNTHFS; -.
DR   Proteomes; UP000001123; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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   InterPro; IPR013473; BrxL.
DR   InterPro; IPR014061; BrxL-like.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF13337; Lon_2; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR02653; Lon_rel_chp; 1.
DR   TIGRFAMs; TIGR02688; TIGR02688; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Protease.
FT   CHAIN           1..694
FT                   /note="Lon-like protease BrxL"
FT                   /id="PRO_0000452160"
SQ   SEQUENCE   694 AA;  77373 MW;  4AB686BBE0A0C114 CRC64;
     MQTHHDLPVS GVSAGEIASE GYDLDALLNQ HFAGRVVRKD LTKQLKEGAN VPVYVLEYLL
     GMYCASDDDD VVEQGLQNVK RILADNYVRP DEAEKVKSLI RERGSYKIID KVSVKLNQKK
     DVYEAQLSNL GIKDALVPSQ MVKDNEKLLT GGIWCMITVN YFFEEGQKTS PFSLMTLKPI
     QMPNMDMEEV FDARKHFNRD QWIDVLLRSV GMEPANIEQR TKWHLITRMI PFVENNYNVC
     ELGPRGTGKS HVYKECSPNS LLVSGGQTTV ANLFYNMASR QIGLVGMWDV VAFDEVAGIT
     FKDKDGVQIM KDYMASGSFS RGRDSIEGKA SMVFVGNINQ SVETLVKTSH LLAPFPAAMI
     DTAFFDRFHA YIPGWEIPKM RPEFFTNRYG LITDYLAEYM REMRKRSFSD AIDKFFKLGN
     NLNQRDVIAV RRTVSGLLKL MHPDGAYSKE DVRVCLTYAM EVRRRVKEQL KKLGGLEFFD
     VNFSYIDNET LEEFFVSVPE QGGSELIPAG MPKPGVVHLV TQAESGMTGL YRFETQMTAG
     NGKHSVSGLG SNTSAKEAIR VGFDYFKGNL NRVSAAAKFS DHEYHLHVVE LHNTGPSTAT
     SLAALIALCS ILLAKPVQEQ MVVLGSMTLG GVINPVQDLA ASLQLAFDSG AKRVLLPMSS
     AMDIPTVPAE LFTKFQVSFY SDPVDAVYKA LGVN