ID   MOAD_BACSU              Reviewed;          77 AA.
AC   O31706; Q7BVS2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Molybdopterin synthase sulfur carrier subunit;
DE   AltName: Full=MPT synthase subunit 1;
DE   AltName: Full=Molybdenum cofactor biosynthesis protein D;
DE   AltName: Full=Molybdopterin-converting factor small subunit;
DE   AltName: Full=Molybdopterin-converting factor subunit 1;
DE   AltName: Full=Sulfur carrier protein MoaD;
GN   Name=moaD; OrderedLocusNames=BSU14310;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Caldwell R.M., Ferrari E.;
RT   "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT   chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Involved in sulfur transfer in the conversion of
CC       molybdopterin precursor Z to molybdopterin. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Forms a
CC       stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation
CC       of MoaD by MoeB. During catalysis MoaD shuttles between the two
CC       heterotetrameric complexes (By similarity). {ECO:0000250}.
CC   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC       adenylated (-COAMP) by MoeB, then thiocarboxylated (-COSH) by IscS.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MoaD family. {ECO:0000305}.
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DR   EMBL; AF012285; AAC24905.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13304.1; -; Genomic_DNA.
DR   PIR; A69659; A69659.
DR   RefSeq; NP_389314.1; NC_000964.3.
DR   RefSeq; WP_003232366.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31706; -.
DR   SMR; O31706; -.
DR   STRING; 224308.BSU14310; -.
DR   jPOST; O31706; -.
DR   PaxDb; O31706; -.
DR   PRIDE; O31706; -.
DR   EnsemblBacteria; CAB13304; CAB13304; BSU_14310.
DR   GeneID; 938785; -.
DR   KEGG; bsu:BSU14310; -.
DR   PATRIC; fig|224308.179.peg.1561; -.
DR   eggNOG; COG1977; Bacteria.
DR   InParanoid; O31706; -.
DR   OMA; HIGCENI; -.
DR   PhylomeDB; O31706; -.
DR   BioCyc; BSUB:BSU14310-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR044672; MOCS2A.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   PANTHER; PTHR33359; PTHR33359; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..77
FT                   /note="Molybdopterin synthase sulfur carrier subunit"
FT                   /id="PRO_0000392066"
FT   MOD_RES         77
FT                   /note="1-thioglycine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         77
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   77 AA;  8104 MW;  FF094BD83DBB75BF CRC64;
     MIKILLFAGL AEQAGTQAIE IDMEQATTDE IKASLKEQYG LESIDTAMIA VNESYVKENT
     SVSSGDTVAI IPPVSGG