OMP5_HAEIN
ID OMP5_HAEIN Reviewed; 353 AA.
AC P43840;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Outer membrane protein P5 {ECO:0000303|PubMed:16905616};
DE Short=OMP P5;
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane protein OmpA;
DE AltName: Full=Outer membrane protein d {ECO:0000303|PubMed:6603458};
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842}; Synonyms=ompP5;
GN OrderedLocusNames=HI_1164;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND IMMUNOLOGICAL SIMILARITY TO OMPA.
RC STRAIN=760705 / Type B;
RX PubMed=6603458; DOI=10.1128/jb.155.2.878-885.1983;
RA van Alphen L., Riemens T., Poolman J., Zanen H.C.;
RT "Characteristics of major outer membrane proteins of Haemophilus
RT influenzae.";
RL J. Bacteriol. 155:878-885(1983).
RN [3]
RP FUNCTION, AND FORMS LARGE AND SMALL PORES.
RC STRAIN=NTHi UC19;
RX PubMed=16905616; DOI=10.1529/biophysj.106.088781;
RA Zakharian E., Reusch R.N.;
RT "Pore characteristics of nontypeable Haemophilus influenzae outer membrane
RT protein P5 in planar lipid bilayers.";
RL Biophys. J. 91:3242-3248(2006).
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 -!- FUNCTION: Reconstitution in planar bilayers with lithium dodecyl
CC sulfate-solublized P5 yields narrow pores (58 pS conductance) with a
CC low probability of opening, whereas n-octyl-bD-glucopyranoside-
CC solubilized P5 forms large pores (1.1 nS conductance) with high open
CC probability. The large pore easily converts to the smaller pore at room
CC temperature; at 42 degrees Celsius the smaller pore converts to the
CC larger one. {ECO:0000269|PubMed:16905616}.
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:6603458}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00842}.
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 -!- MISCELLANEOUS: Cross reacts with antisera againt E.coli OmpA.
CC {ECO:0000269|PubMed:6603458}.
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; L42023; AAC22819.1; -; Genomic_DNA.
DR PIR; C64187; C64187.
DR RefSeq; NP_439322.1; NC_000907.1.
DR RefSeq; WP_010869142.1; NC_000907.1.
DR AlphaFoldDB; P43840; -.
DR SMR; P43840; -.
DR STRING; 71421.HI_1164; -.
DR EnsemblBacteria; AAC22819; AAC22819; HI_1164.
DR KEGG; hin:HI_1164; -.
DR PATRIC; fig|71421.8.peg.1216; -.
DR eggNOG; COG2885; Bacteria.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_031536_0_0_6; -.
DR OMA; HDTGFYG; -.
DR PhylomeDB; P43840; -.
DR BioCyc; HINF71421:G1GJ1-1198-MON; -.
DR Proteomes; UP000000579; 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-UniRule.
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 3: Inferred from homology;
KW Cell outer membrane; Disulfide bond; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT CHAIN 22..353
FT /note="Outer membrane protein P5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000020107"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 58..69
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 77..85
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 104..115
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 120..128
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 158..167
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 172..179
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 205..213
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DOMAIN 227..353
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 80
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 175
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 326..338
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ SEQUENCE 353 AA; 37744 MW; 64ACB3E7BFF96B39 CRC64;
MKKTAIALVV AGLAAASVAQ AAPQENTFYA GVKAGQASFH DGLRALAREY KVGYHRNSFT
YGVFGGYQIL NQNNLGLAVE LGYDDFGRAK GREKGKTVVK HTNHGTHLSL KGSYEVLEGL
DVYGKAGVAL VRSDYKLYNE NSSTLKKLGE HHRARASGLF AVGAEYAVLP ELAVRLEYQW
LTRVGKYRPQ DKPNTALNYN PWIGSINAGI SYRFGQGAAP VVAAPEVVSK TFSLNSDVTF
AFGKANLKPQ AQATLDSIYG EMSQVKSAKV AVAGYTDRIG SDAFNVKLSQ ERADSVANYF
VAKGVAADAI SATGYGKANP VTGATCDQVK GRKALIACFA PDRRVEIAVN GTK
