GSPB_ECOLI
ID GSPB_ECOLI Reviewed; 139 AA.
AC P03825; Q2M6Y7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative general secretion pathway protein B {ECO:0000305};
GN Name=gspB {ECO:0000303|PubMed:11118204};
GN Synonyms=pinO {ECO:0000303|PubMed:1925011, ECO:0000303|PubMed:1938934},
GN pioO {ECO:0000312|EMBL:BAE77969.1}, pno; OrderedLocusNames=b3322, JW3284;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7037196; DOI=10.1016/0092-8674(81)90303-2;
RA Olins P.O., Nomura M.;
RT "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide
RT sequence at the start of the operon.";
RL Cell 26:205-211(1981).
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 IDENTIFICATION.
RX PubMed=1925011; DOI=10.1016/0923-2508(91)90021-2;
RA Guzman E.C., Jimenez-Sanchez A.;
RT "A calcium-binding protein that may be required for the initiation of
RT chromosome replication in Escherichia coli.";
RL Res. Microbiol. 142:137-140(1991).
RN [5]
RP IDENTIFICATION.
RX PubMed=1938934; DOI=10.1128/jb.173.23.7409.1991;
RA Guzman E.C., Jimenez-Sanchez A.;
RT "Location of pinO, a new gene located between tufA and rpsJ, on the
RT physical map of the Escherichia coli chromosome.";
RL J. Bacteriol. 173:7409-7409(1991).
RN [6]
RP LACK OF EXPRESSION OF THE OPERON.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA Francetic O., Pugsley A.P.;
RT "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT 12 encodes functional proteins.";
RL J. Bacteriol. 178:3544-3549(1996).
RN [7]
RP LACK OF EXPRESSION OF THE OPERON, FUNCTION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT "Expression of the endogenous type II secretion pathway in Escherichia coli
RT leads to chitinase secretion.";
RL EMBO J. 19:6697-6703(2000).
CC -!- FUNCTION: Part of a cryptic operon that encodes proteins involved in
CC type II secretion pathway in other organisms, but is not expressed in
CC strain K12 under standard laboratory conditions (PubMed:8655552). May
CC play a regulatory role under conditions of derepressed gsp gene
CC expression (PubMed:11118204). {ECO:0000269|PubMed:11118204,
CC ECO:0000305|PubMed:8655552}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- CAUTION: Was originally identified as the 11.3 kDa PinO protein, a
CC calcium-binding protein synthesized in the absence of isoleucine in
CC relA stains, which may be required for the initiation of chromosome
CC replication (PubMed:1925011, PubMed:1938934). But GspB is predicted to
CC be 15.9 kDa and has isoleucine residues, and there is no evidence that
CC gspB encodes the PinO peptide or that it binds calcium. {ECO:0000305,
CC ECO:0000305|PubMed:1925011, ECO:0000305|PubMed:1938934}.
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DR EMBL; V00344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U18997; AAA58119.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76347.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77969.1; -; Genomic_DNA.
DR PIR; E65125; QQECRP.
DR RefSeq; NP_417781.1; NC_000913.3.
DR RefSeq; WP_000461450.1; NZ_SSZK01000040.1.
DR AlphaFoldDB; P03825; -.
DR SMR; P03825; -.
DR BioGRID; 4261294; 169.
DR STRING; 511145.b3322; -.
DR PaxDb; P03825; -.
DR PRIDE; P03825; -.
DR EnsemblBacteria; AAC76347; AAC76347; b3322.
DR EnsemblBacteria; BAE77969; BAE77969; BAE77969.
DR GeneID; 947826; -.
DR KEGG; ecj:JW3284; -.
DR KEGG; eco:b3322; -.
DR PATRIC; fig|511145.12.peg.3415; -.
DR EchoBASE; EB1243; -.
DR eggNOG; ENOG5033BEH; Bacteria.
DR HOGENOM; CLU_152450_0_0_6; -.
DR OMA; QSMWHER; -.
DR BioCyc; EcoCyc:EG11263-MON; -.
DR PRO; PR:P03825; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..139
FT /note="Putative general secretion pathway protein B"
FT /id="PRO_0000058445"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 93..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1..66
FT /note="MFEFYIAAREQKETGHPGIFSRQKHSTIIYVICLLLICLWFAGMVLVGGYAR
FT QLWVLWIVKAEVTV -> MTDLPVVCRNGAGWWVCQAAMGALDSKSRSHL (in Ref.
FT 1; V00344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 139 AA; 15876 MW; 36DE3301CB52EE47 CRC64;
MFEFYIAARE QKETGHPGIF SRQKHSTIIY VICLLLICLW FAGMVLVGGY ARQLWVLWIV
KAEVTVEAET PAFKQSTQHY FFKKQPLPVV ESVEEEDDPG VAVENAPSSS EDEENTVEES
EEKAGLRERV KNALNELER