Gene Ontology annotation through association of InterPro records with GO terms

SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly.

In E. coli, SufE transfers SufS-derived sulfur to SufB (requiring SufC), and SufB acts as a site for Fe-S cluster assembly.

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.

Crystal structure of E. coli SufBCD shows an ABC-protein architecture with two SufC ATPases and a SufB-SufD heterodimer; ATPase driven conformational change is proposed to drive cluster assembly.

PMID:28839209

Mapping the key residues of SufB and SufD essential for biosynthesis of iron-sulfur clusters.

E. coli SufB Cys254 is essential for sulfur transfer from SufE; SufB Cys405 and Glu434 with SufD His360 form the de novo cluster site.

PMID:24321018

Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein.

In Firmicutes the SUF system uses SufU rather than SufE as the sulfur acceptor of SufS, with SufB, SufC and SufD as candidate scaffold components.

PMID:20097860

SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis.

SufU is proposed to be the Fe-S cluster scaffold of the B. subtilis SUF system.

"SufS-dependent formation of holo-SufU suggests that SufU functions as an Fe/S cluster scaffold protein tightly cooperating with the SufS cysteine desulfurase."

PMID:24009606

Interaction between the genomes of Lactococcus lactis and phages of the P335 species

Uses llmg_1969 (sufB) only as a landmark of a prophage integration site; no functional data.

PMID:24936909

Oxidative stress enhances the expression of sulfur assimilation genes: preliminary insights on the Enterococcus faecalis iron-sulfur cluster machinery regulation

The E. faecalis sufCDSUB operon (sufB ortholog EF2390, 78.7% identity) is induced by H2O2.

PMID:25485887

Molecular investigation of iron-sulfur cluster assembly scaffolds under stress.

E. coli SufB binds a [2Fe-2S] cluster that is more stable than the IscU cluster under oxidative stress and iron limitation.

PMID:33234689

Genes Contributing to the Unique Biology and Intrinsic Antibiotic Resistance of Enterococcus faecalis.

PMID:19187533

Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein.

PMID:17307855

Complete genome sequence of the prototype lactic acid bacterium Lactococcus lactis subsp. cremoris MG1363.

file:LACLM/sufB/sufB-uniprot.txt

UniProtKB entry A2RMK5 (llmg_1969)

file:LACLM/sufB/sufB-bioinformatics/RESULTS.md

sufB identity, family, residue conservation and operon context analysis

The KBase protein NZ_LKLC01000161.1_58 is identical to A2RMK5, and TIGR01980 matches A2RMK5 over residues 14-461.
A2RMK5 conserves E. coli SufB C254, C405 and E434 (as C236, C380, E409) and lies in a sufC-sufD-sufS-sufU-sufB operon.