ID   OMP1_IGNH4              Reviewed;          85 AA.
AC   A8ABZ0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Major outer membrane protein 1;
DE            Short=Ihomp1;
DE   AltName: Full=Outer membrane protein Imp1227;
DE   Flags: Precursor;
GN   Name=ihomp1; Synonyms=imp1227; OrderedLocusNames=Igni_1266;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-31, AND SUBCELLULAR LOCATION.
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=18584152; DOI=10.1007/s00203-008-0399-x;
RA   Burghardt T., Saller M., Gurster S., Muller D., Meyer C., Jahn U.,
RA   Hochmuth E., Deutzmann R., Siedler F., Babinger P., Wirth R., Huber H.,
RA   Rachel R.;
RT   "Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus
RT   hospitalis: the major cytosolic and membrane proteins.";
RL   Arch. Microbiol. 190:379-394(2008).
RN   [3]
RP   PROTEIN SEQUENCE OF 19-28, SUBCELLULAR LOCATION, AND SUBUNIT.
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=17163971; DOI=10.1111/j.1365-2958.2006.05509.x;
RA   Burghardt T., Nather D.J., Junglas B., Huber H., Rachel R.;
RT   "The dominating outer membrane protein of the hyperthermophilic Archaeum
RT   Ignicoccus hospitalis: a novel pore-forming complex.";
RL   Mol. Microbiol. 63:166-176(2007).
CC   -!- FUNCTION: The most abundant protein of the outer membrane, it forms a
CC       pore through it.
CC   -!- SUBUNIT: Forms extremely stable complexes with apparent masses of 150,
CC       50, 45 and 38 kDa. Found in a ring-shaped complex of 7 nm diameter with
CC       a 2 nm channel through the middle. Complete denaturation requires
CC       temperatures over 110 degrees Celsius. {ECO:0000269|PubMed:17163971}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:17163971,
CC       ECO:0000305|PubMed:18584152}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:17163971, ECO:0000305|PubMed:18584152}.
CC   -!- MISCELLANEOUS: Ignicoccus hospitalis is unique in having an energized
CC       outer membrane while ATP synthesis occurs within the periplasmic space.
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DR   EMBL; CP000816; ABU82442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ABZ0; -.
DR   STRING; 453591.Igni_1266; -.
DR   TCDB; 1.A.63.1.1; the ignicoccus outer membrane Alpha-helical porin (i-omp) family.
DR   EnsemblBacteria; ABU82442; ABU82442; Igni_1266.
DR   KEGG; iho:Igni_1266; -.
DR   HOGENOM; CLU_2504911_0_0_2; -.
DR   Proteomes; UP000000262; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:17163971,
FT                   ECO:0000269|PubMed:18584152"
FT   CHAIN           19..85
FT                   /note="Major outer membrane protein 1"
FT                   /id="PRO_0000415942"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   85 AA;  8388 MW;  2DE479A679784D3E CRC64;
     MEAREVEEMR RSRLLTLGGI GYTAVIALAA LVLVMGALGL VLKVAAAAGA LPSEVAKVAN
     ALPGLKASVD ANPAAGSLSS VSVST