ID   GSPN_PECCC              Reviewed;         248 AA.
AC   P31710;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Type II secretion system protein N;
DE            Short=T2SS protein N;
DE   AltName: Full=General secretion pathway protein N;
DE   AltName: Full=Pectic enzymes secretion protein OutN;
GN   Name=outN;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
RN   [2]
RP   TOPOLOGY.
RX   PubMed=8065262; DOI=10.1111/j.1365-2958.1994.tb01033.x;
RA   Reeves P.J., Douglas P., Salmond G.P.C.;
RT   "Beta-lactamase topology probe analysis of the OutO NMePhe peptidase, and
RT   six other Out protein components of the Erwinia carotovora general
RT   secretion pathway apparatus.";
RL   Mol. Microbiol. 12:445-457(1994).
CC   -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC       general secretion pathway, GSP) for the export of proteins (By
CC       similarity). Required for the translocation of the multiple pectic
CC       enzymes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the GSP N family. {ECO:0000305}.
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DR   EMBL; X70049; CAA49655.1; -; Genomic_DNA.
DR   PIR; S32868; S32868.
DR   AlphaFoldDB; P31710; -.
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; IPR000645; T2SS_GspN_CS.
DR   InterPro; IPR022792; T2SS_protein-GspN.
DR   Pfam; PF01203; T2SSN; 1.
DR   PROSITE; PS01142; T2SP_N; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..248
FT                   /note="Type II secretion system protein N"
FT                   /id="PRO_0000195053"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8065262"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        28..248
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:8065262"
SQ   SEQUENCE   248 AA;  26772 MW;  43798853EE5405BE CRC64;
     MKLKSGIVTG VALVLAYGLF LASYAPARLL TAVPLPAGMV VAEAAGTLWQ GSLQRFSWRT
     LTLDDVHWNI TFSDFMPALD IAFKNPEGIA GRGIIRGWQR AQFYQWQLSV PAGYLFSHMR
     FIVPIGAEGN VQLNLQEATV DRSGCQSLDA NVTWPGARVK TPLGGLVLAT PQATLRCQQG
     ALEANLRQTS SHLQLSGKGS VTPKGEYRFT GQLSSGNDLP ATMKKLLATT GKANEQGART
     LNFQGRLL