PAGN_SALTY
ID PAGN_SALTY Reviewed; 239 AA.
AC Q8ZRJ9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Outer membrane protein PagN;
DE AltName: Full=Adhesin/invasin protein PagN;
DE Flags: Precursor;
GN Name=pagN; Synonyms=iviVI-A; OrderedLocusNames=STM0306;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=9922242; DOI=10.1128/jb.181.3.799-807.1999;
RA Heithoff D.M., Conner C.P., Hentschel U., Govantes F., Hanna P.C.,
RA Mahan M.J.;
RT "Coordinate intracellular expression of Salmonella genes induced during
RT infection.";
RL J. Bacteriol. 181:799-807(1999).
RN [3]
RP FUNCTION IN VIRULENCE, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=18778463; DOI=10.1186/1471-2180-8-142;
RA Lambert M.A., Smith S.G.;
RT "The PagN protein of Salmonella enterica serovar Typhimurium is an adhesin
RT and invasin.";
RL BMC Microbiol. 8:142-142(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RC STRAIN=LT2;
RX PubMed=19552707; DOI=10.1111/j.1574-6968.2009.01666.x;
RA Lambert M.A., Smith S.G.;
RT "The PagN protein mediates invasion via interaction with proteoglycan.";
RL FEMS Microbiol. Lett. 297:209-216(2009).
CC -!- FUNCTION: Haemagglutinin that facilitates the adhesion to and invasion
CC of epithelial mammalian cells. Utilizes heparinated proteoglycan as a
CC receptor to successfully invade host cells.
CC {ECO:0000269|PubMed:18778463, ECO:0000269|PubMed:19552707}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:18778463,
CC ECO:0000269|PubMed:19552707}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18778463, ECO:0000269|PubMed:19552707}.
CC -!- INDUCTION: Induced by both low pH and low Mg(2+) via the PhoQ/PhoP two-
CC component regulatory system. Responds to general intracellular signals
CC that are present both in initial and in progressive stages of
CC infection. {ECO:0000269|PubMed:9922242}.
CC -!- DOMAIN: All four putative extracellular loops are crucial for invasion
CC of mammalian cells. {ECO:0000269|PubMed:19552707}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL19263.1; -; Genomic_DNA.
DR RefSeq; NP_459304.1; NC_003197.2.
DR RefSeq; WP_000787603.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRJ9; -.
DR STRING; 99287.STM0306; -.
DR PaxDb; Q8ZRJ9; -.
DR EnsemblBacteria; AAL19263; AAL19263; STM0306.
DR GeneID; 1251825; -.
DR KEGG; stm:STM0306; -.
DR PATRIC; fig|99287.12.peg.325; -.
DR HOGENOM; CLU_057473_1_0_6; -.
DR OMA; YGAVRIN; -.
DR PhylomeDB; Q8ZRJ9; -.
DR BioCyc; SENT99287:STM0306-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR027385; OMP_b-brl.
DR Pfam; PF13505; OMP_b-brl; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..239
FT /note="Outer membrane protein PagN"
FT /id="PRO_0000407308"
FT TOPO_DOM 23..26
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..36
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..76
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..81
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..92
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..132
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..148
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..185
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..190
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..200
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..239
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 25708 MW; 84A99F284DB5A84A CRC64;
MKNFFAVCII PLVVAWSATA SAKEGIYITG KAGTSVVNVY GINSTFSQDE IVNGHATLPD
RTKGVFGGGV AIGYDFYDPF QLPVRLELDT TFRGETDAKG GQDIIAFGDP VHINVKNQVR
MTTYMVNGYY DFHNSTAFTP YISAGVGLAH VKLSNNTIPV GFGINETLSA SKNNFAWGAG
IGAKYAVTDN IMIDASYKYI NAGKVSISKN HYAGDEHTAY DADTKAASND FMLGITYAF
