ID   OMP5_GLAPU              Reviewed;          15 AA.
AC   P85410;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Outer membrane protein P5 {ECO:0000303|Ref.1};
DE            Short=OMP P5;
DE   AltName: Full=Outer membrane protein A;
DE   Flags: Fragment;
GN   Name=ompA {ECO:0000305};
OS   Glaesserella parasuis (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=738;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=SW114 {ECO:0000269|Ref.1}, and SW140 {ECO:0000269|Ref.1};
RA   McVicker J.K.;
RT   "The identification and characterization of P5 and P2 colonization proteins
RT   in Haemophilus parasuis and the targeted binding of carcinoembryonic
RT   antigen (CEA).";
RL   Thesis (2004), Iowa State University, United States.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=IA84-297755 {ECO:0000269|PubMed:16971306};
RX   PubMed=16971306; DOI=10.1080/10826060600912658;
RA   McVicker J.K., Tabatabai L.B.;
RT   "Isolation and characterization of the P5 adhesin protein of Haemophilus
RT   parasuis serotype 5.";
RL   Prep. Biochem. Biotechnol. 36:363-374(2006).
CC   -!- FUNCTION: Does not bind carcinoembryonic antigen (CEA).
CC       {ECO:0000269|PubMed:16971306}.
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.
CC       {ECO:0000250|UniProtKB:P0A910}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P0A910}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:P0A910, ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P0A910, ECO:0000305}.
CC   -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC       some bacteria confer sensitivity to phage and/or colicins.
CC       {ECO:0000250|UniProtKB:P0A910}.
CC   -!- MISCELLANEOUS: On a 2D-gel the determined pI of this protein is: 5.5,
CC       its MW is: 32 kDa. {ECO:0000269|PubMed:16971306}.
CC   -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC       OmpA family. {ECO:0000305}.
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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:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Ion transport; Membrane;
KW   Porin; Transmembrane; Transmembrane beta strand; Transport.
FT   CHAIN           1..>15
FT                   /note="Outer membrane protein P5"
FT                   /id="PRO_0000317225"
FT   TRANSMEM        6..>15
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A910"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1496 MW;  1130FE757CC822DE CRC64;
     APQANSFYVG AKAGD