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 27-MAR-2024, entry version 122.
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; Pseudomonadota; 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; 511145-b1254; -.
DR EnsemblBacteria; AAC74336; AAC74336; b1254.
DR GeneID; 83576450; -.
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 OrthoDB; 9788219at2; -.
DR PhylomeDB; P0A710; -.
DR BioCyc; EcoCyc:EG11122-MONOMER; -.
DR PRO; PR:P0A710; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR HAMAP; MF_00189; YciB; 1.
DR InterPro; IPR006008; YciB.
DR NCBIfam; TIGR00997; ispZ; 1.
DR PANTHER; PTHR36917:SF1; INNER MEMBRANE-SPANNING PROTEIN YCIB; 1.
DR PANTHER; PTHR36917; INTRACELLULAR SEPTATION PROTEIN A-RELATED; 1.
DR Pfam; PF04279; IspA; 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
//
