ID   BRXA_MAGSA              Reviewed;         199 AA.
AC   Q2W5N3;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=BREX protein BrxA {ECO:0000305};
GN   Name=brxA {ECO:0000305}; OrderedLocusNames=amb2038;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
RN   [2] {ECO:0007744|PDB:3BHW}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-199.
RC   STRAIN=AMB-1 / ATCC 700264;
RA   Bonanno J.B., Dickey M., Bain K.T., Lau C., Romero R., Smith D.,
RA   Wasserman S., Sauder J.M., Burley S.K., Almo S.C.;
RT   "Crystal structure of an uncharacterized protein from Magnetospirillum
RT   magneticum.";
RL   Submitted (NOV-2007) to the PDB data bank.
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. {ECO:0000250|UniProtKB:P0DUF6}.
CC   -!- SIMILARITY: Belongs to the BrxA family. {ECO:0000305}.
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DR   EMBL; AP007255; BAE50842.1; -; Genomic_DNA.
DR   RefSeq; WP_011384441.1; NC_007626.1.
DR   PDB; 3BHW; X-ray; 1.50 A; A/B=2-199.
DR   PDBsum; 3BHW; -.
DR   AlphaFoldDB; Q2W5N3; -.
DR   SMR; Q2W5N3; -.
DR   STRING; 342108.amb2038; -.
DR   EnsemblBacteria; BAE50842; BAE50842; amb2038.
DR   KEGG; mag:amb2038; -.
DR   HOGENOM; CLU_087567_0_1_5; -.
DR   OMA; FYKLKQV; -.
DR   OrthoDB; 1116618at2; -.
DR   EvolutionaryTrace; Q2W5N3; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3540.10; -; 1.
DR   InterPro; IPR014948; BrxA.
DR   InterPro; IPR023137; BrxA_sf.
DR   Pfam; PF08849; DUF1819; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Reference proteome.
FT   CHAIN           1..199
FT                   /note="BREX protein BrxA"
FT                   /id="PRO_0000452154"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           17..29
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           33..41
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           81..95
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           97..105
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           120..133
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           143..158
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           177..185
FT                   /evidence="ECO:0007829|PDB:3BHW"
FT   HELIX           189..195
FT                   /evidence="ECO:0007829|PDB:3BHW"
SQ   SEQUENCE   199 AA;  22963 MW;  717C7AA5DD278FDA CRC64;
     MAEPRYKADI GGGSLKLPES RIIAGLLLEG VTEDQWRHAI EVENVLQRRS PGTAKRQSSL
     MRNRLETMGP ELWQMVRDGS TQVAIQAVFA AAIKHSTLLG DFLDLVVRDQ FRMFRPDLPR
     KMWDQYLEQC RNRDPLMPVW QDSTANKLAD CVYRILVEVG YITDSKTYRL KSVRISGEVM
     SYLRENNEQY VIRCIQVSI