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Database: UniProt
Entry: Q0I4B1_HISS1
LinkDB: Q0I4B1_HISS1
Original site: Q0I4B1_HISS1 
ID   Q0I4B1_HISS1            Unreviewed;       355 AA.
AC   Q0I4B1;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Outer membrane protein A {ECO:0000256|ARBA:ARBA00029539, ECO:0000256|HAMAP-Rule:MF_00842};
DE   AltName: Full=Outer membrane porin A {ECO:0000256|HAMAP-Rule:MF_00842};
GN   Name=hagA {ECO:0000313|EMBL:ABI25310.1};
GN   Synonyms=ompA {ECO:0000256|HAMAP-Rule:MF_00842};
GN   OrderedLocusNames=HS_1035 {ECO:0000313|EMBL:ABI25310.1};
OS   Histophilus somni (strain 129Pt) (Haemophilus somnus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914 {ECO:0000313|EMBL:ABI25310.1};
RN   [1] {ECO:0000313|EMBL:ABI25310.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129PT {ECO:0000313|EMBL:ABI25310.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Dalin E., Tice H., Pitluck S., Brettin T.S., Bruce D., Challacombe J.F.,
RA   Chertkov O., Detter J.C., Gilna P., Han S., Misra M., Tapia R.,
RA   Thayer N.N., Xie G., Inzana T.J., Duncan A.J., Siddaramppa S.,
RA   Richardson P.;
RT   "Complete genome sequence of Haemophilus somnus 129PT.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00842}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_00842}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|HAMAP-Rule:MF_00842};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571,
CC       ECO:0000256|HAMAP-Rule:MF_00842}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC       some bacteria confer sensitivity to phage and/or colicins.
CC       {ECO:0000256|HAMAP-Rule:MF_00842}.
CC   -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC       OmpA family. {ECO:0000256|ARBA:ARBA00005710, ECO:0000256|HAMAP-
CC       Rule:MF_00842}.
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DR   EMBL; CP000436; ABI25310.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0I4B1; -.
DR   KEGG; hso:HS_1035; -.
DR   eggNOG; COG2885; Bacteria.
DR   eggNOG; COG3637; Bacteria.
DR   HOGENOM; CLU_031536_0_0_6; -.
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:monoatomic ion transmembrane transport; IEA:UniProtKB-UniRule.
DR   CDD; cd07185; OmpA_C-like; 1.
DR   Gene3D; 2.40.160.20; -; 1.
DR   Gene3D; 3.30.1330.60; OmpA-like domain; 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; IPR036737; OmpA-like_sf.
DR   InterPro; IPR000498; OmpA-like_TM_dom.
DR   PANTHER; PTHR30329:SF23; LIPOPROTEIN YIAD-RELATED; 1.
DR   PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR   Pfam; PF00691; OmpA; 1.
DR   Pfam; PF01389; OmpA_membrane; 1.
DR   PRINTS; PR01021; OMPADOMAIN.
DR   PRINTS; PR01022; OUTRMMBRANEA.
DR   SUPFAM; SSF103088; OmpA-like; 1.
DR   SUPFAM; SSF56925; OMPA-like; 1.
DR   PROSITE; PS51123; OMPA_2; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00842};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_00842};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00842};
KW   Porin {ECO:0000256|ARBA:ARBA00023114, ECO:0000256|HAMAP-Rule:MF_00842};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00842};
KW   Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452,
KW   ECO:0000256|HAMAP-Rule:MF_00842};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00842}.
FT   DOMAIN          229..355
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51123"
FT   SITE            88
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT   SITE            181
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
FT   DISULFID        328..340
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00842"
SQ   SEQUENCE   355 AA;  38108 MW;  B47F9A30FED69142 CRC64;
     MLNFLIINIE EIQMKKTIIA LSIAGFVASV QAAPQANTFY AGAKAGWASF HDGLNQFEDS
     SQKKGTVRNS VAYGIFGGYQ ITDHVAVELG SEYFGQAKGR KDKDEAKHTA QGMQLGLKAS
     YPVLEGLDIY GRVGAALIRS NYLNVEKFES GKDVKNTLKV SPVFAAGVEY SLPSLPELAL
     RLEYQWVKGV GKALKKSSGE RLDYTPSIGA VTLGLSYRFG QKPVMAPEVV NKVFSLNSDV
     NFAFAKDTLK PEAQQTLDGV YGEIAQLKTA QVSVAGYTDR IGSDASNLKL SQRRADTVAN
     YLVSKGVAQD AISAVGYGEA NPVTGAKCDA VKGRKALIAC LAEDRRVEIS VKGSK
//
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