ID   SELA_CAMJJ              Reviewed;         440 AA.
AC   A1W0Z5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000255|HAMAP-Rule:MF_00423};
GN   OrderedLocusNames=CJJ81176_1380;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC         selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC         Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC         ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00423};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00423};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
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DR   EMBL; CP000538; EAQ72930.1; -; Genomic_DNA.
DR   RefSeq; WP_002858009.1; NC_008787.1.
DR   AlphaFoldDB; A1W0Z5; -.
DR   SMR; A1W0Z5; -.
DR   STRING; 354242.CJJ81176_1380; -.
DR   EnsemblBacteria; EAQ72930; EAQ72930; CJJ81176_1380.
DR   KEGG; cjj:CJJ81176_1380; -.
DR   eggNOG; COG1921; Bacteria.
DR   HOGENOM; CLU_038142_1_0_7; -.
DR   OMA; GATNRTH; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_00423; SelA; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR018319; SelA-like.
DR   InterPro; IPR004534; SelA_trans.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00474; selA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Selenium;
KW   Transferase.
FT   CHAIN           1..440
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_1000050358"
FT   MOD_RES         282
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   440 AA;  50612 MW;  DCA149D0275C0C83 CRC64;
     MNKFRTFPQI NTLIEDESLK SYPFYIKAFF CKKVVAKLKE NFFQDEISKD KLLLEIKKEI
     KTFYRKDLQS VINASGVVIH TNLGRSVIHE ELYEACKDII CNYSNVEFDL ENGKRGSRYA
     LVLEKLKMLF ECEDALVVNN NAAAVFLVLN SLCYDKEVIS SRGELVEIGG SFRVPEVIKA
     AGVKLCEVGT SNKTHLKDYE QAINENTALI LKTHKSNFAL MGFHSEVNIK DLHELAKEKE
     LLSYYDLGSG WCENLNEKLI KNEPKIRKLV QECDILSFSG DKLFGSVQAG IILGKKELIE
     KLKQNQLLRM LRVDKLTLSF LNESLKAYLQ KDYEKIITLK LLNDDLSFIE KKALRVQKEL
     KFQTQLKKSK SLVGGGSMPD KSLDTYILTF QGDALKLQTR FRKENIIGRI ENDEFVLDFR
     TIRENELQKL ILTINQMENL