ID   WBKC_BRUA2              Reviewed;         259 AA.
AC   Q2YML4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=GDP-perosamine N-formyltransferase {ECO:0000250|UniProtKB:F8WJP6};
DE            EC=2.1.2.14 {ECO:0000250|UniProtKB:F8WJP6};
GN   Name=wbkC {ECO:0000303|PubMed:20580469};
GN   OrderedLocusNames=BAB1_0540 {ECO:0000312|EMBL:CAJ10496.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=20580469; DOI=10.1016/j.vaccine.2010.06.023;
RA   Lacerda T.L., Cardoso P.G., Augusto de Almeida L., Camargo I.L.,
RA   Afonso D.A., Trant C.C., Macedo G.C., Campos E., Cravero S.L.,
RA   Salcedo S.P., Gorvel J.P., Oliveira S.C.;
RT   "Inactivation of formyltransferase (wbkC) gene generates a Brucella abortus
RT   rough strain that is attenuated in macrophages and in mice.";
RL   Vaccine 28:5627-5634(2010).
CC   -!- FUNCTION: Involved in the lipopolysaccharide (LPS) O-antigen
CC       biosynthesis (PubMed:20580469). Catalyzes the transfer of a formyl
CC       group to GDP-perosamine, leading to the formation of GDP-N-
CC       formylperosamine (By similarity). Is critical for full bacterial
CC       virulence (PubMed:20580469). {ECO:0000250|UniProtKB:F8WJP6,
CC       ECO:0000269|PubMed:20580469}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + GDP-alpha-D-perosamine =
CC         (6S)-5,6,7,8-tetrahydrofolate + GDP-N-formyl-alpha-D-perosamine +
CC         H(+); Xref=Rhea:RHEA:68588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:73996, ChEBI:CHEBI:176524;
CC         EC=2.1.2.14; Evidence={ECO:0000250|UniProtKB:F8WJP6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68589;
CC         Evidence={ECO:0000250|UniProtKB:F8WJP6};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000269|PubMed:20580469}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:F8WJP6}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutant lacks lipopolysaccharide O-side
CC       chain. In vivo, mutants are attenuated in C57BL/6 and IRF-1 knockout
CC       mice. In bone marrow-derived macrophages (BMDM), mutants are
CC       attenuated, cannot reach a replicative niche and induce higher levels
CC       of IL-12 and TNF-alpha when compared to parental smooth strains.
CC       {ECO:0000269|PubMed:20580469}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; AM040264; CAJ10496.1; -; Genomic_DNA.
DR   RefSeq; WP_002963675.1; NZ_KN046823.1.
DR   SMR; Q2YML4; -.
DR   STRING; 359391.BAB1_0540; -.
DR   EnsemblBacteria; CAJ10496; CAJ10496; BAB1_0540.
DR   GeneID; 45123991; -.
DR   GeneID; 55590265; -.
DR   KEGG; bmf:BAB1_0540; -.
DR   PATRIC; fig|359391.11.peg.2578; -.
DR   HOGENOM; CLU_033347_2_0_5; -.
DR   OMA; FTHESPY; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
PE   3: Inferred from homology;
KW   Lipopolysaccharide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..259
FT                   /note="GDP-perosamine N-formyltransferase"
FT                   /id="PRO_0000455051"
FT   BINDING         89..91
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:F8WJP6"
FT   BINDING         139..143
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:F8WJP6"
SQ   SEQUENCE   259 AA;  29128 MW;  DC92E53DE2F8A444 CRC64;
     MAIAPNTRVL VAGYGLPAEF CVTTLIGMGV EIDKIAVATH REDNRNCGLH SMLRLRNIQF
     TTAAANSEEF YEFGANFDPD MIISMHYRSL IPGRFLKLAK KGSVNLHPSL LPAYRGTNSV
     AWVIINGESE TGFSYHRMDE NFDTGAILLQ ERISVEETDT AFSLFHRQIA RAMLRLEEVI
     LKLDQGDPGF AQLGEASYYA RELPFGGVID PRWSEVQIDR FIRAMFFPPF PPAVLKIDGK
     VYYVPSIDIY RSLMRGIPS