PORA_CAMJE
ID PORA_CAMJE Reviewed; 424 AA.
AC P80672; Q0P8Z7; Q9PN38;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Major outer membrane protein;
DE AltName: Full=Porin;
DE Flags: Precursor;
GN Name=porA; OrderedLocusNames=Cj1259;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP PROTEIN SEQUENCE OF 23-101 AND 106-424.
RC STRAIN=K22;
RX PubMed=9163918; DOI=10.1111/j.1574-6968.1997.tb10362.x;
RA Schroeder W.F.K.J., Moser I.;
RT "Primary structure analysis and adhesion studies on the major outer
RT membrane protein of Campylobacter jejuni.";
RL FEMS Microbiol. Lett. 150:141-147(1997).
RN [3]
RP PROTEIN SEQUENCE OF 23-53.
RC STRAIN=85H;
RX PubMed=7543469; DOI=10.1128/jb.177.15.4266-4271.1995;
RA Bolla J.-M., Loret E., Zalewski M., Pages J.-M.;
RT "Conformational analysis of the Campylobacter jejuni porin.";
RL J. Bacteriol. 177:4266-4271(1995).
CC -!- FUNCTION: Assembles to form a functional porin. May be one of the
CC structures responsible for adhesion to intestinal cells.
CC -!- SUBUNIT: Homotrimer and monomer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane.
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DR EMBL; AL111168; CAL35374.1; -; Genomic_DNA.
DR PIR; E81333; E81333.
DR RefSeq; WP_010891919.1; NC_002163.1.
DR RefSeq; YP_002344650.1; NC_002163.1.
DR AlphaFoldDB; P80672; -.
DR SMR; P80672; -.
DR STRING; 192222.Cj1259; -.
DR PaxDb; P80672; -.
DR PRIDE; P80672; -.
DR ABCD; P80672; 3 sequenced antibodies.
DR EnsemblBacteria; CAL35374; CAL35374; Cj1259.
DR GeneID; 905550; -.
DR KEGG; cje:Cj1259; -.
DR PATRIC; fig|192222.6.peg.1242; -.
DR eggNOG; COG4773; Bacteria.
DR HOGENOM; CLU_679130_0_0_7; -.
DR OMA; PQLWLAY; -.
DR PHI-base; PHI:6661; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR008439; Campylo_MOMP.
DR Pfam; PF05538; Campylo_MOMP; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Membrane; Porin; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:7543469,
FT ECO:0000269|PubMed:9163918"
FT CHAIN 23..424
FT /note="Major outer membrane protein"
FT /id="PRO_0000025214"
FT CONFLICT 52
FT /note="V -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="E -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="K -> KK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..418
FT /note="RL -> LR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 45688 MW; 4AA0DDB40B61679C CRC64;
MKLVKLSLVA ALAAGAFSAA NATPLEEAIK DVDVSGVLRY RYDTGNFDKN FVNNSNLNNS
KQDHKYRAQV NFSAAIADNF KAFVQFDYNA ADGGYGANGI KNDQKGLFVR QLYLTYTNED
VATSVIAGKQ QLNLIWTDNA IDGLVGTGVK VVNNSIDGLT LAAFAVDSFM AAEQGADLLE
HSNISTTSNQ APFKVDSVGN LYGAAAVGSY DLAGGQFNPQ LWLAYWDQVA FFYAVDAAYS
TTIFDGINWT LEGAYLGNSL DSELDDKTHA NGNLFALKGS IEVNGWDASL GGLYYGDKEK
ASTVVIEDQG NLGSLLAGEE IFYTTGSRLN GDTGRNIFGY VTGGYTFNET VRVGADFVYG
GTKTEAANHL GGGKKLEAVA RVDYKYSPKL NFSAFYSYVN LDQGVNTNES ADHSTVRLQA
LYKF