OMP53_HAEIF
ID OMP53_HAEIF Reviewed; 359 AA.
AC P45996;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Outer membrane protein P5 {ECO:0000303|PubMed:7909539};
DE Short=OMP P5;
DE AltName: Full=Fimbrin {ECO:0000303|PubMed:7909539};
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane protein A;
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842}; Synonyms=ompP5;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-41 AND 234-248,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=NTHi 1128;
RX PubMed=7909539; DOI=10.1128/iai.62.5.2002-2020.1994;
RA Sirakova T., Kolattukudy P.E., Murwin D., Billy J., Leake E., Lim D.,
RA Demaria T., Bakaletz L.;
RT "Role of fimbriae expressed by nontypeable Haemophilus influenzae in
RT pathogenesis of and protection against otitis media and relatedness of the
RT fimbrin subunit to outer membrane protein A.";
RL Infect. Immun. 62:2002-2020(1994).
CC -!- FUNCTION: Acts as a fimbriae subunit, allowing adhesion to host cells.
CC {ECO:0000269|PubMed:7909539}.
CC -!- FUNCTION: With TolR probably plays a role in maintaining the position
CC of the peptidoglycan cell wall in the periplasm. Acts as a porin with
CC low permeability that allows slow penetration of small solutes; an
CC internal gate slows down solute passage. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00842, ECO:0000269|PubMed:7909539}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00842}. Fimbrium
CC {ECO:0000269|PubMed:7909539}. Note=Antisera against this protein label
CC the whole length of fimbriae. {ECO:0000269|PubMed:7909539}.
CC -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC some bacteria confer sensitivity to phage and/or colicins.
CC {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- DISRUPTION PHENOTYPE: No fimbrae seen on bacteria, the outer membrane
CC blebs significantly, bacterial adhesion to human oropharyngeal cells
CC decreases about 65%, significantly reduced ear infections in
CC chinchilla. {ECO:0000269|PubMed:7909539}.
CC -!- BIOTECHNOLOGY: Immunization of chinchillas with this protein provides
CC partial protection against subsequent infection, suggesting it might be
CC a useful vaccine candidate. {ECO:0000269|PubMed:7909539}.
CC -!- MISCELLANEOUS: Non-typeable Haemophilus influenzae (NTHi) is a primary
CC pathogen in otitis media (inflammation of the middle ear).
CC {ECO:0000269|PubMed:7909539}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
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DR EMBL; L08448; AAA24959.1; -; Genomic_DNA.
DR AlphaFoldDB; P45996; -.
DR SMR; P45996; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_00842; OmpA; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR002368; OmpA.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR000498; OmpA-like_TM_dom.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Direct protein sequencing;
KW Disulfide bond; Fimbrium; Ion transport; Membrane; Porin; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842,
FT ECO:0000269|PubMed:7909539"
FT CHAIN 22..359
FT /note="Outer membrane protein P5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000020109"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 64..75
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 83..91
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 110..121
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 126..134
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 164..173
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 178..185
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 211..219
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DOMAIN 233..359
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 86
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 181
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 332..344
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ SEQUENCE 359 AA; 38340 MW; 576B1C59B4818C37 CRC64;
MKKTAIALVV AGLAAASVAQ AAPQENTFYA GVKAGQGSFH DGINNNGAIK KGLSSSNYGY
RRNTFTYGVF GGYQILNQDN FGLAAELGYD DFGRAKLREA GKPKAKHTNH GAYLSLKGSY
EVLDGLDVYG KAGVALVRSD YKFYEDANGT RDHKKGRHTA RASGLFAVGA EYAVLPELAV
RLEYQWLTRV GKYRPQDKPN TAINYNPWIG CINAGISYRF GQGEAPVVAA PEMVSKTFSL
NSDVTFAFGK ANLKPQAQAT LDSVYGEISQ VKSRKVAVAG YTNRIGSDAF NVKLSQERAD
SVANYFVAKG VAADAISATG YGEANPVTGA TCDQVKGRKA LIACLAPDRR VEIAVNGTK
