GSPM_ECOLI
ID GSPM_ECOLI Reviewed; 153 AA.
AC P36678; Q2M6Z9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative type II secretion system protein M;
DE Short=T2SS protein M;
DE AltName: Full=Putative general secretion pathway protein M;
DE AltName: Full=Transport protein PshM;
GN Name=gspM; Synonyms=hopZ, pshM; OrderedLocusNames=b3334, JW5704;
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=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(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 LACK OF EXPRESSION.
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 [5]
RP LACK OF EXPRESSION, 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: Inner membrane component of the type II secretion system
CC required for the energy-dependent secretion of extracellular factors
CC such as proteases and toxins from the periplasm. Plays a role in the
CC complex assembly and recruits GspL resulting in a stable complex in the
CC inner membrane. Provides thus a link between the energy-providing GspE
CC protein in the cytoplasm and the rest of the T2SS machinery.
CC {ECO:0000250|UniProtKB:P25061}.
CC -!- SUBUNIT: Type II secretion system is composed of four main components:
CC the outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus (By
CC similarity). Forms homodimers (By similarity). Interacts with GspL.
CC Interacts with GspE and GspF (By similarity).
CC {ECO:0000250|UniProtKB:P25061, ECO:0000250|UniProtKB:P41851,
CC ECO:0000250|UniProtKB:Q00514}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P25061}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P25061}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC in type II secretion machinery in other organisms, but is not expressed
CC in strain K12.
CC -!- SIMILARITY: Belongs to the GSP M family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58131.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC36927.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L28106; AAC36927.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA58131.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76359.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77957.1; -; Genomic_DNA.
DR PIR; A65127; A65127.
DR RefSeq; NP_417793.2; NC_000913.3.
DR RefSeq; WP_001295161.1; NZ_STEB01000038.1.
DR AlphaFoldDB; P36678; -.
DR BioGRID; 4262464; 145.
DR STRING; 511145.b3334; -.
DR PaxDb; P36678; -.
DR PRIDE; P36678; -.
DR EnsemblBacteria; AAC76359; AAC76359; b3334.
DR EnsemblBacteria; BAE77957; BAE77957; BAE77957.
DR GeneID; 58459571; -.
DR GeneID; 947841; -.
DR KEGG; ecj:JW5704; -.
DR KEGG; eco:b3334; -.
DR PATRIC; fig|1411691.4.peg.3397; -.
DR EchoBASE; EB2091; -.
DR eggNOG; COG3149; Bacteria.
DR eggNOG; ENOG502ZF85; Bacteria.
DR HOGENOM; CLU_1710496_0_0_6; -.
DR OMA; KCHERCN; -.
DR BioCyc; EcoCyc:EG12173-MON; -.
DR BioCyc; MetaCyc:EG12173-MON; -.
DR PRO; PR:P36678; -.
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.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR007690; T2SS_GspM.
DR InterPro; IPR023229; T2SS_M_periplasmic_sf.
DR Pfam; PF04612; T2SSM; 1.
DR SUPFAM; SSF103054; SSF103054; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..153
FT /note="Putative type II secretion system protein M"
FT /id="PRO_0000207323"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..153
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
SQ SEQUENCE 153 AA; 17234 MW; 8BF3991FB160383C CRC64;
MIKSWWAEKS TSEKQIVAAL AVLSLGVFCW LGVIKPIDTY IAEHQSHAQK IKKDIKWMQD
QASTHGLLGH PALTQPIKNI LLEEAKRENL AITLENGPDN TLTIHPVTAP LENVSRWLTT
AQVTYGIVIE DLQFTLAGNE EITLRHLSFR EQQ
