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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
 
 
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