DCRB_ECOLI
ID DCRB_ECOLI Reviewed; 185 AA.
AC P0AEE1; P37620; P76699; Q2M7D5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Inner membrane lipoprotein DcrB {ECO:0000255|HAMAP-Rule:MF_02248, ECO:0000303|PubMed:33431434};
DE Flags: Precursor;
GN Name=dcrB {ECO:0000255|HAMAP-Rule:MF_02248, ECO:0000303|PubMed:8752353};
GN Synonyms=yhhR; OrderedLocusNames=b3472, JW5682;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN PHAGE C1 INFECTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=8752353; DOI=10.1128/jb.178.17.5309-5315.1996;
RA Likhacheva N.A., Samsonov V.V., Samsonov V.V., Sineoky S.P.;
RT "Genetic control of the resistance to phage C1 of Escherichia coli K-12.";
RL J. Bacteriol. 178:5309-5315(1996).
RN [5]
RP FUNCTION IN PHAGE INFECTION (MICROBIAL INFECTION), AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12558182; DOI=10.1016/s0923-2508(02)01375-x;
RA Samsonov V.V., Samsonov V.V., Sineoky S.P.;
RT "DcrA and dcrB Escherichia coli genes can control DNA injection by phages
RT specific for BtuB and FhuA receptors.";
RL Res. Microbiol. 153:639-646(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30368949; DOI=10.1111/mmi.14157;
RA Mychack A., Amrutha R.N., Chung C., Cardenas Arevalo K., Reddy M.,
RA Janakiraman A.;
RT "A synergistic role for two predicted inner membrane proteins of
RT Escherichia coli in cell envelope integrity.";
RL Mol. Microbiol. 111:317-337(2019).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33431434; DOI=10.1128/jb.00640-20;
RA Mychack A., Janakiraman A.;
RT "Defects in the first step of lipoprotein maturation underlie the synthetic
RT lethality of Escherichia coli lacking the inner membrane proteins YciB and
RT DcrB.";
RL J. Bacteriol. 0:0-0(2021).
CC -!- FUNCTION: Plays a role in cell envelope biogenesis, maintenance of cell
CC envelope integrity and membrane homeostasis (PubMed:30368949,
CC PubMed:33431434). Essential for lipoprotein maturation under conditions
CC where membrane fluidity may be altered (PubMed:33431434).
CC {ECO:0000269|PubMed:30368949, ECO:0000269|PubMed:33431434}.
CC -!- FUNCTION: (Microbial infection) Involved in phage C1 and phage C6
CC infection (PubMed:8752353, PubMed:12558182). Participates in phage DNA
CC transport pathways in cooperation with different outer membrane
CC receptors, including FhuA and BtuB (PubMed:12558182). Is probably
CC required in the second stage of phage adsorption, the DNA injection
CC process. Participates in the formation or opening of diffusion channels
CC through the outer membrane after phage adsorption (PubMed:12558182).
CC DcrB probably only increases the efficiency of SdaC/DcrA action
CC (PubMed:12558182). {ECO:0000269|PubMed:12558182,
CC ECO:0000269|PubMed:8752353}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02248};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02248}; Periplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_02248}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to phage C1
CC adsorption defect. Mutation does not impair vitamin B12 utilization
CC (PubMed:8752353). Mutant is resistant to phage C6 (PubMed:12558182).
CC Null mutant is not viable when grown at low temperatures, conditions
CC which impact membrane fluidity (PubMed:33431434). Cells lacking both
CC yciB and dcrB display pleiotropic defects, including morphological
CC changes, elevated amounts of lipopolysaccharide, membrane vesiculation,
CC reduced proton motive force, accumulation of outer membrane proteins at
CC the inner membrane, and dynamic shrinking and extension of the
CC cytoplasmic membrane accompanied by lysis and cell death
CC (PubMed:30368949). Double mutant also displays a reduction in membrane
CC fluidity and a marked sensitivity to copper ions (PubMed:33431434). It
CC accumulates additional forms of Lpp and shows aberrant localization of
CC Lpp due to inefficient lipid modification at the first step in
CC lipoprotein maturation (PubMed:33431434). {ECO:0000269|PubMed:12558182,
CC ECO:0000269|PubMed:30368949, ECO:0000269|PubMed:33431434,
CC ECO:0000269|PubMed:8752353}.
CC -!- SIMILARITY: Belongs to the DcrB family. {ECO:0000255|HAMAP-
CC Rule:MF_02248, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18447.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18447.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76497.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77821.1; -; Genomic_DNA.
DR RefSeq; NP_417929.4; NC_000913.3.
DR RefSeq; WP_001245295.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P0AEE1; -.
DR SMR; P0AEE1; -.
DR BioGRID; 4262924; 131.
DR BioGRID; 852292; 4.
DR DIP; DIP-36187N; -.
DR IntAct; P0AEE1; 9.
DR STRING; 511145.b3472; -.
DR TCDB; 9.B.357.1.1; the bacterial envelope biogenesis (beb) family.
DR SWISS-2DPAGE; P0AEE1; -.
DR jPOST; P0AEE1; -.
DR PaxDb; P0AEE1; -.
DR PRIDE; P0AEE1; -.
DR EnsemblBacteria; AAC76497; AAC76497; b3472.
DR EnsemblBacteria; BAE77821; BAE77821; BAE77821.
DR GeneID; 66672644; -.
DR GeneID; 947983; -.
DR KEGG; ecj:JW5682; -.
DR KEGG; eco:b3472; -.
DR PATRIC; fig|511145.12.peg.3571; -.
DR EchoBASE; EB2132; -.
DR eggNOG; ENOG502Z932; Bacteria.
DR HOGENOM; CLU_125378_0_0_6; -.
DR InParanoid; P0AEE1; -.
DR OMA; ACDNSDT; -.
DR PhylomeDB; P0AEE1; -.
DR BioCyc; EcoCyc:G7767-MON; -.
DR PRO; PR:P0AEE1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_02248; DcrB; 1.
DR InterPro; IPR046406; DcrB.
DR InterPro; IPR014894; DcrB/EagT6.
DR Pfam; PF08786; DcrB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02248"
FT CHAIN 20..185
FT /note="Inner membrane lipoprotein DcrB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02248"
FT /id="PRO_0000021094"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02248"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02248"
SQ SEQUENCE 185 AA; 19787 MW; 8412B6A4028750B2 CRC64;
MRNLVKYVGI GLLVMGLAAC DDKDTNATAQ GSVAESNATG NPVNLLDGKL SFSLPADMTD
QSGKLGTQAN NMHVWSDATG QKAVIVIMGD DPKEDLAVLA KRLEDQQRSR DPQLQVVTNK
AIELKGHKMQ QLDSIISAKG QTAYSSVILG NVGNQLLTMQ ITLPADDQQK AQTTAENIIN
TLVIQ
