EIPB_BRUA2
ID EIPB_BRUA2 Reviewed; 280 AA.
AC Q2YRJ0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Cell envelope integrity protein EipB {ECO:0000303|PubMed:30936371};
DE Flags: Precursor;
GN Name=eipB {ECO:0000303|PubMed:30936371};
GN OrderedLocusNames=BAB1_1186 {ECO:0000312|EMBL:CAJ11142.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000312|Proteomes:UP000002719};
RN [1] {ECO:0000312|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000312|Proteomes:UP000002719};
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] {ECO:0007744|PDB:6NTR}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-280, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DISULFIDE BOND, AND MUTAGENESIS
RP OF CYS-69 AND CYS-278.
RX PubMed=30936371; DOI=10.1128/jb.00134-19;
RA Herrou J., Willett J.W., Fiebig A., Czyz D.M., Cheng J.X., Ultee E.,
RA Briegel A., Bigelow L., Babnigg G., Kim Y., Crosson S.;
RT "Brucella Periplasmic Protein EipB Is a Molecular Determinant of Cell
RT Envelope Integrity and Virulence.";
RL J. Bacteriol. 201:JB.00134-JB.00134(2019).
CC -!- FUNCTION: Functions in the periplasm to maintain cell envelope
CC integrity. {ECO:0000269|PubMed:30936371}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30936371}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:30936371}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to the cell envelope stressors
CC ampicillin, deoxycholate, and ethylenediaminetetraacetic acid (EDTA)
CC (PubMed:30936371). Decreases virulence in a mouse model of infection
CC (PubMed:30936371). {ECO:0000269|PubMed:30936371}.
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DR EMBL; AM040264; CAJ11142.1; -; Genomic_DNA.
DR RefSeq; WP_002966849.1; NZ_KN046823.1.
DR PDB; 6NTR; X-ray; 2.10 A; A/B/C/D=29-280.
DR PDBsum; 6NTR; -.
DR AlphaFoldDB; Q2YRJ0; -.
DR SMR; Q2YRJ0; -.
DR STRING; 359391.BAB1_1186; -.
DR EnsemblBacteria; CAJ11142; CAJ11142; BAB1_1186.
DR GeneID; 45124538; -.
DR GeneID; 55590845; -.
DR KEGG; bmf:BAB1_1186; -.
DR PATRIC; fig|359391.11.peg.84; -.
DR HOGENOM; CLU_064490_0_0_5; -.
DR OMA; FRFVTQI; -.
DR PhylomeDB; Q2YRJ0; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0043163; P:cell envelope organization; IMP:UniProtKB.
DR InterPro; IPR015000; EipB-like.
DR Pfam; PF08904; EipB_like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30936371"
FT CHAIN 25..280
FT /note="Cell envelope integrity protein EipB"
FT /id="PRO_5004219355"
FT DISULFID 69..278
FT /evidence="ECO:0000269|PubMed:30936371"
FT MUTAGEN 69
FT /note="C->S: Abolishes disulfide bond formation; when
FT associated with S-278."
FT /evidence="ECO:0000269|PubMed:30936371"
FT MUTAGEN 278
FT /note="C->S: Abolishes disulfide bond formation; when
FT associated with S-69."
FT /evidence="ECO:0000269|PubMed:30936371"
FT CONFLICT 250
FT /note="L -> M (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31355 MW; 10B3A1563936BCFD CRC64;
MRFVRIAAAA SGATVFMWAG FAGAASAASA VRLVPHRAIY DLTLDRADEK SGISGLTGRM
VYEFNGSACE GYTTNFRFVT RVDMDEQPQR VTDQQTTTFE DADGKDFRFV NKTFVDKELV
KEVRGDAKLE DGKTVVKLSK PKENTLDLKG TQFPTRHMEE LIGKAEAGQK FYQTTLFDAS
EDADRVVATT VVVGKQQAVP DDETKVMGKF SKDQVWPVTI AYFDDKEQQD GMPIYRINFK
LYRNGITRDL TMDYGDFSMR GKLVKLDIYD TGKNKTGCSK