ID   SPSS_METTP              Reviewed;         388 AA.
AC   A0B5D0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {ECO:0000255|HAMAP-Rule:MF_01675};
DE            EC=2.5.1.73 {ECO:0000255|HAMAP-Rule:MF_01675};
DE   AltName: Full=Sep-tRNA:Cys-tRNA synthase {ECO:0000255|HAMAP-Rule:MF_01675};
DE            Short=SepCysS {ECO:0000255|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=Mthe_0102;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC       cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000255|HAMAP-Rule:MF_01675}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-
CC         cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA-
CC         COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
CC   -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK13904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000477; ABK13904.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0B5D0; -.
DR   SMR; A0B5D0; -.
DR   STRING; 349307.Mthe_0102; -.
DR   EnsemblBacteria; ABK13904; ABK13904; Mthe_0102.
DR   KEGG; mtp:Mthe_0102; -.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   Proteomes; UP000000674; Chromosome.
DR   GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR   InterPro; IPR008829; SepSecS/SepCysS.
DR   PANTHER; PTHR43586:SF3; PTHR43586:SF3; 1.
DR   Pfam; PF05889; SepSecS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02539; SepCysS; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..388
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT                   /id="PRO_0000359459"
FT   BINDING         89..90
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         195
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         218..220
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   388 AA;  43487 MW;  0C52BCCAB11FE741 CRC64;
     MPSSITSKLD KFRCMKRSIS EINLDPLQRG GILTPEARAA LVEWGDGYSV CDFCEGMLDR
     VRNPPVEEFV HEILPRFLDV DDVRITHGAR EGMYAAMHSL CDAGDYIVAD GNAHYTTVLA
     AERAGLEISY VENSGEPEYT INPEGYREAI RDAADQGYRV SMAVLTYPDG NYGNLVDARR
     VAEICHEEGV PLLLNGAYSI GRMPVSAREL DADIVVGSGH KSMASSGPIG VLGAKQEYAD
     IIFRRSKSKK NKEVELLGCT VRGAGLLTMM ASFPHVLERV GRWQEEVDKA RWFSSELEEL
     GIEQQGEKPH NHDLMFFKSE RLYEISKSAR KGRYFLYHEL KDRGICGIKP GLTRQFKLST
     YLIPREDLER VVSAFHEIIE MGSRVEAE