ID   SNAB_STRPR              Reviewed;         277 AA.
AC   P54993;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Pristinamycin IIA synthase subunit B;
DE            Short=PIIA synthase subunit B;
GN   Name=snaB;
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP92;
RX   PubMed=7665509; DOI=10.1128/jb.177.18.5206-5214.1995;
RA   Blanc V., Lagneaux D., Didier P., Gil P., Lacroix P., Crouzet J.;
RT   "Cloning and analysis of structural genes from Streptomyces
RT   pristinaespiralis encoding enzymes involved in the conversion of
RT   pristinamycin IIB to pristinamycin IIA (PIIA): PIIA synthase and
RT   NADH:riboflavin 5'-phosphate oxidoreductase.";
RL   J. Bacteriol. 177:5206-5214(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-23 AND 122-136.
RX   PubMed=7665508; DOI=10.1128/jb.177.18.5199-5205.1995;
RA   Thibaut D., Ratet N., Bisch D., Faucher D., Debussche L., Blanche F.;
RT   "Purification of the two-enzyme system catalyzing the oxidation of the D-
RT   proline residue of pristinamycin IIB during the last step of pristinamycin
RT   IIA biosynthesis.";
RL   J. Bacteriol. 177:5199-5205(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of the proline residue of
CC       pristinamycin IIB (PIIB) to pristinamycin IIA (PIIA).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SUBUNIT: Heterodimer of two subunits, SnaA and SnaB.
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DR   EMBL; U21215; AAA83565.1; -; Genomic_DNA.
DR   RefSeq; WP_050791658.1; NZ_CP011340.1.
DR   AlphaFoldDB; P54993; -.
DR   SMR; P54993; -.
DR   STRING; 38300.SPRI_0183; -.
DR   OrthoDB; 1653347at2; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7665508"
FT   CHAIN           2..277
FT                   /note="Pristinamycin IIA synthase subunit B"
FT                   /id="PRO_0000072001"
SQ   SEQUENCE   277 AA;  28764 MW;  C3C33D1726F817B5 CRC64;
     MTAPILVATL DTRGPAATLG TITRAVRAAE AAGFDAVLID DRAAAGVQGR FETTTLTAAL
     AAVTEHIGLI TAPLPADQAP YHVSRITASL DHLAHGRTGW LASTDTTDPE GRTGELIDVV
     RGLWDSFDDD AFVHDRADGL YWRLPAVHQL DHQGRHFDVA GPLNVARPPQ GHPVVAVTGP
     ALAAAADLVL LDEAADAASV KQQAPHAKIL LPLPGPAAEL PADSPADGFT VALTGSDDPV
     LAALAARPGR PDRTAATTLR ERLGLARPES RHALTTA