OMPC_SHIFL
ID OMPC_SHIFL Reviewed; 373 AA.
AC A0A2S4MYF8; Q7C0S7; Q83QU7;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Outer membrane protein C;
DE AltName: Full=Porin OmpC;
DE Flags: Precursor;
GN Name=ompC; OrderedLocusNames=SF2299;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP SUBUNIT (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL INFECTION),
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=22386055; DOI=10.1016/j.virol.2012.01.040;
RA Parent K.N., Gilcrease E.B., Casjens S.R., Baker T.S.;
RT "Structural evolution of the P22-like phages: comparison of Sf6 and P22
RT procapsid and virion architectures.";
RL Virology 427:177-188(2012).
RN [3]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=24673644; DOI=10.1111/mmi.12536;
RA Parent K.N., Erb M.L., Cardone G., Nguyen K., Gilcrease E.B., Porcek N.B.,
RA Pogliano J., Baker T.S., Casjens S.R.;
RT "OmpA and OmpC are critical host factors for bacteriophage Sf6 entry in
RT Shigella.";
RL Mol. Microbiol. 92:47-60(2014).
RN [4] {ECO:0007744|PDB:3NB3}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.00 ANGSTROMS), PROTEIN SEQUENCE OF
RP 22-26, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=M94;
RX PubMed=21071053; DOI=10.1016/j.virol.2010.10.030;
RA Zhao H., Sequeira R.D., Galeva N.A., Tang L.;
RT "The host outer membrane proteins OmpA and OmpC are associated with the
RT Shigella phage Sf6 virion.";
RL Virology 409:319-327(2011).
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane. {ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Serves as a less-preferential secondary
CC receptor during phage Sf6 infection; infection requires both
CC lipopolysaccharide (LPS) and (in the absence of OmpA) OmpC can serve as
CC the secondary receptor. {ECO:0000269|PubMed:24673644}.
CC -!- SUBUNIT: Homotrimer. Forms mixed heterotrimers with OmpF and with PhoE;
CC other mixed heterotrimers are also probable.
CC {ECO:0000250|UniProtKB:P06996}.
CC -!- SUBUNIT: (Microbial infection) Upon infection with phage Sf6 associates
CC with the mature bacteriophage capsid (PubMed:21071053,
CC PubMed:22386055). Was originally suggested to be within the
CC bacteriophage capsid (PubMed:21071053). This has been disproven
CC (PubMed:22386055). {ECO:0000269|PubMed:21071053,
CC ECO:0000269|PubMed:22386055}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P06996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21071053}.
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle. Note=(Microbial infection)
CC Upon infection with phage Sf6 is found in extracellular vesicles that
CC associate with the tails of mature bacteriophage particles.
CC {ECO:0000269|PubMed:22386055}.
CC -!- DISRUPTION PHENOTYPE: No effect on propagation of phage Sf6
CC (PubMed:22386055). Upon infection with phage Sf6, single deletion
CC mutant has a wild-type level of small plaques with no change in
CC bacterial survival; double ompA-ompC deletions have about 10-fold fewer
CC plaques, survive infection considerably better than wild-type, are
CC infected more slowly and have fewer extracellular vesicles associated
CC with mature bacteriophage (PubMed:24673644).
CC {ECO:0000269|PubMed:22386055, ECO:0000269|PubMed:24673644}.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; AE005674; AAN43817.1; -; Genomic_DNA.
DR RefSeq; NP_708110.1; NC_004337.2.
DR RefSeq; WP_000865562.1; NZ_WPGW01000022.1.
DR PDB; 3NB3; EM; -; D=22-367.
DR PDBsum; 3NB3; -.
DR AlphaFoldDB; A0A2S4MYF8; -.
DR SMR; A0A2S4MYF8; -.
DR STRING; 198214.SF2299; -.
DR EnsemblBacteria; AAN43817; AAN43817; SF2299.
DR GeneID; 1026756; -.
DR GeneID; 58388744; -.
DR KEGG; sfl:SF2299; -.
DR PATRIC; fig|198214.7.peg.2753; -.
DR HOGENOM; CLU_058202_0_0_6; -.
DR OMA; DNKENSW; -.
DR OrthoDB; 1064531at2; -.
DR Proteomes; UP000001006; 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:0034220; P:ion transmembrane transport; IEA:InterPro.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001897; Porin_gammaproteobac.
DR InterPro; IPR001702; Porin_Gram-ve.
DR InterPro; IPR013793; Porin_Gram-ve_CS.
DR Pfam; PF00267; Porin_1; 1.
DR PRINTS; PR00183; ECOLIPORIN.
DR PRINTS; PR00182; ECOLNEIPORIN.
DR PROSITE; PS00576; GRAM_NEG_PORIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Host-virus interaction; Ion transport; Membrane; Porin; Reference proteome;
KW Signal; Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:21071053"
FT CHAIN 22..373
FT /note="Outer membrane protein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000447415"
FT TRANSMEM 34..42
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 54..63
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 74..84
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 92..101
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 107..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 142..154
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 164..171
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 197..203
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 208..215
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 244..250
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 255..262
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 272..288
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 294..301
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 325..332
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 337..344
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TRANSMEM 365..372
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT REGION 116..133
FT /note="Loop L3; may constrict the pore"
FT /evidence="ECO:0000250|UniProtKB:P06996"
SQ SEQUENCE 373 AA; 41402 MW; 15711869390ACCB2 CRC64;
MKVKVLSLLV PALLVAGAAN AAEVYNKDGN KLDLYGKVDG LHYFSDDKSV DGDQTYMRLG
FKGETQVTDQ LTGYGQWEYQ IQGNSAENEN NSWTRVAFAG LKFQDVGSFD YGRNYGVVYD
VTSWTDVLPE FGGDTYGSDN FMQQRGNGFA TYRSTDFFGL VDGLNFAVQY QGKNGSPEGE
GMTNNGREAL RQNGDGVGGS ITYDYEGFGI GAAVSSSKRT DDQNFGLNRY DERYIGNGDR
AETYTGGLKY DANNIYLAAQ YTQTYNATRV GNLGWANKAQ NFEAVAQYQF DFGLRPSLAY
LQSKGKNLGV INGRNYDDED ILKYVDVGAT YYFNKNMSTY VDYKINLLDD NQFTRDAGIN
TDNIVALGLV YQF
