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YCIB_ECOLI
ID   YCIB_ECOLI              Reviewed;         179 AA.
AC   P0A710; P21366; P94721; P94725; P94735; P94738;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Inner membrane-spanning protein YciB {ECO:0000255|HAMAP-Rule:MF_00189, ECO:0000303|PubMed:33431434};
GN   Name=yciB {ECO:0000255|HAMAP-Rule:MF_00189}; Synonyms=ispZ;
GN   OrderedLocusNames=b1254, JW1246;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3058546; DOI=10.1093/genetics/120.2.345;
RA   Stoltzfus A., Leslie J.F., Milkman R.;
RT   "Molecular evolution of the Escherichia coli chromosome. I. Analysis of
RT   structure and natural variation in a previously uncharacterized region
RT   between trp and tonB.";
RL   Genetics 120:345-358(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12, and Various ECOR strains;
RA   Milkman R.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [4]
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   [5]
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   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [7]
RP   RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP   INFECTION), AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA   Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT   "Contact-dependent growth inhibition toxins exploit multiple independent
RT   cell-entry pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
RN   [8]
RP   FUNCTION, INTERACTION WITH ZIPA, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=26391555; DOI=10.1111/gtc.12299;
RA   Badaluddin N.A., Kitakawa M.;
RT   "Escherichia coli inner membrane protein YciB interacts with ZipA that is
RT   important for cell division.";
RL   Genes Cells 20:956-965(2015).
RN   [9]
RP   FUNCTION, INTERACTION WITH CELL ELONGATION AND CELL DIVISION PROTEINS,
RP   SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=26454142; DOI=10.1111/1348-0421.12330;
RA   Li G., Badaluddin N.A., Kitakawa M.;
RT   "Characterization of inner membrane protein YciB in Escherichia coli: YciB
RT   interacts with cell elongation and division proteins.";
RL   Microbiol. Immunol. 59:700-704(2015).
RN   [10]
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   [11]
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:26391555,
CC       PubMed:26454142, PubMed:30368949, PubMed:33431434). Required for the
CC       normal cell elongation (PubMed:26391555). May participate in the cell
CC       division process (PubMed:26391555). Important for the septum site
CC       localization of the essential divisome protein ZipA (PubMed:26391555).
CC       {ECO:0000269|PubMed:26391555, ECO:0000269|PubMed:26454142,
CC       ECO:0000269|PubMed:30368949, ECO:0000269|PubMed:33431434}.
CC   -!- FUNCTION: (Microbial infection) Probably transports the toxic C-
CC       terminal region of CdiA from E.coli strain 869 across the inner
CC       membrane to the cytoplasm, where CdiA degrades DNA. Toxin transport is
CC       strain-specific, mutations in this gene do not confer resistance to
CC       several other tested CdiA toxins. {ECO:0000269|PubMed:26305955}.
CC   -!- SUBUNIT: Interact with various proteins involved in cell elongation and
CC       cell division (PubMed:26454142). Directly interacts with ZipA
CC       (PubMed:26391555). {ECO:0000269|PubMed:26391555,
CC       ECO:0000269|PubMed:26454142}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00189, ECO:0000269|PubMed:15919996,
CC       ECO:0000269|PubMed:26391555, ECO:0000269|PubMed:26454142}; Multi-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_00189,
CC       ECO:0000269|PubMed:26454142, ECO:0000305|PubMed:15919996}.
CC       Note=Distributed in the inner membrane through the whole cell.
CC       {ECO:0000269|PubMed:26391555}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is shorter than wild type and
CC       shows abnormal localization of ZipA, an essential protein of cell
CC       division (PubMed:26391555). Deletion mutant is sensitive to low
CC       osmolarity (PubMed:26454142). Disruption confers resistance to cellular
CC       contact-dependent growth inhibition (CDI) CdiA of E.coli strain 869,
CC       but not to a series of other CdiA toxins tested (PubMed:26305955).
CC       Cells lacking both yciB and dcrB display pleiotropic defects, including
CC       morphological changes, elevated amounts of lipopolysaccharide, membrane
CC       vesiculation, reduced proton motive force, accumulation of outer
CC       membrane proteins at the inner membrane, and dynamic shrinking and
CC       extension of the cytoplasmic membrane accompanied by lysis and cell
CC       death (PubMed:30368949). Double mutant also displays a reduction in
CC       membrane fluidity and a marked sensitivity to copper ions
CC       (PubMed:33431434). It accumulates additional forms of Lpp and shows
CC       aberrant localization of Lpp due to inefficient lipid modification at
CC       the first step in lipoprotein maturation (PubMed:33431434).
CC       {ECO:0000269|PubMed:26305955, ECO:0000269|PubMed:26391555,
CC       ECO:0000269|PubMed:26454142, ECO:0000269|PubMed:30368949,
CC       ECO:0000269|PubMed:33431434}.
CC   -!- SIMILARITY: Belongs to the YciB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00189}.
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DR   EMBL; X13583; CAA31924.1; -; Genomic_DNA.
DR   EMBL; U24195; AAB60067.1; -; Genomic_DNA.
DR   EMBL; U24196; AAB60075.1; -; Genomic_DNA.
DR   EMBL; U24197; AAB60083.1; -; Genomic_DNA.
DR   EMBL; U24198; AAB60091.1; -; Genomic_DNA.
DR   EMBL; U24199; AAB60099.1; -; Genomic_DNA.
DR   EMBL; U24200; AAB60107.1; -; Genomic_DNA.
DR   EMBL; U24201; AAB60115.1; -; Genomic_DNA.
DR   EMBL; U24202; AAB60123.1; -; Genomic_DNA.
DR   EMBL; U24203; AAB60131.1; -; Genomic_DNA.
DR   EMBL; U24204; AAB60139.1; -; Genomic_DNA.
DR   EMBL; U24205; AAB60147.1; -; Genomic_DNA.
DR   EMBL; U24206; AAB60155.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74336.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14786.1; -; Genomic_DNA.
DR   PIR; S07799; S07799.
DR   PIR; T45503; T45503.
DR   RefSeq; NP_415770.1; NC_000913.3.
DR   RefSeq; WP_000808667.1; NZ_STEB01000005.1.
DR   AlphaFoldDB; P0A710; -.
DR   BioGRID; 4262998; 140.
DR   STRING; 511145.b1254; -.
DR   TCDB; 9.B.357.1.1; the bacterial envelope biogenesis (beb) family.
DR   PaxDb; P0A710; -.
DR   PRIDE; P0A710; -.
DR   EnsemblBacteria; AAC74336; AAC74336; b1254.
DR   EnsemblBacteria; BAA14786; BAA14786; BAA14786.
DR   GeneID; 67417427; -.
DR   GeneID; 946228; -.
DR   KEGG; ecj:JW1246; -.
DR   KEGG; eco:b1254; -.
DR   PATRIC; fig|1411691.4.peg.1029; -.
DR   EchoBASE; EB1112; -.
DR   eggNOG; COG2917; Bacteria.
DR   HOGENOM; CLU_089554_2_0_6; -.
DR   InParanoid; P0A710; -.
DR   OMA; AWVNFKL; -.
DR   PhylomeDB; P0A710; -.
DR   BioCyc; EcoCyc:EG11122-MON; -.
DR   PRO; PR:P0A710; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   HAMAP; MF_00189; YciB; 1.
DR   InterPro; IPR006008; YciB.
DR   PANTHER; PTHR36917; PTHR36917; 1.
DR   Pfam; PF04279; IspA; 1.
DR   TIGRFAMs; TIGR00997; ispZ; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..179
FT                   /note="Inner membrane-spanning protein YciB"
FT                   /id="PRO_0000206531"
FT   TOPO_DOM        1..21
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00189"
FT   TOPO_DOM        43..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00189"
FT   TOPO_DOM        71..75
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00189"
FT   TOPO_DOM        97..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00189"
FT   TOPO_DOM        142..148
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00189"
FT   TOPO_DOM        170..179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996,
FT                   ECO:0000269|PubMed:26454142"
FT   VARIANT         99
FT                   /note="P -> Q (in strain: ECOR 31)"
FT   VARIANT         110
FT                   /note="T -> M (in strain: ECOR 28)"
FT   VARIANT         111
FT                   /note="L -> V (in strain: ECOR 60)"
FT   VARIANT         114
FT                   /note="P -> S (in strain: ECOR 52)"
FT   VARIANT         117
FT                   /note="S -> L (in strain: ECOR 28)"
SQ   SEQUENCE   179 AA;  20790 MW;  6A52B2D9CA996EEF CRC64;
     MKQFLDFLPL VVFFAFYKIY DIYAATAALI VATAIVLIYS WVRFRKVEKM ALITFVLVVV
     FGGLTLFFHN DEFIKWKVTV IYALFAGALL VSQWVMKKPL IQRMLGKELT LPQPVWSKLN
     LAWAVFFILC GLANIYIAFW LPQNIWVNFK VFGLTALTLI FTLLSGIYIY RHMPQEDKS
 
 
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