ID   HOPP_HALSX              Reviewed;         366 AA.
AC   A9ZM27;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Monosaccharide porin {ECO:0000305};
DE   AltName: Full=Major outer membrane protein HopP {ECO:0000303|PubMed:15162397};
DE   Flags: Precursor;
GN   Name=hopP {ECO:0000312|EMBL:BAF96703.1, ECO:0000312|EMBL:BAI63216.1};
OS   Halomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1486246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=40;
RA   Tokunaga H., Furukawa M., Tokunaga M.;
RT   "Cloning and expression of the porin gene from Halomonas sp. strain 40.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=40;
RA   Tokunaga H., Furukawa M., Tokunaga M.;
RT   "Cloning and expression of the porin gene from moderately halophilic
RT   bacteria.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 22-36, AND SUBCELLULAR LOCATION.
RC   STRAIN=40;
RX   PubMed=15162397; DOI=10.1002/jobm.200310343;
RA   Tokunaga H., Mitsuo K., Kamekura M., Tokunaga M.;
RT   "Major outer membrane proteins in moderately halophilic eubacteria of
RT   genera Chromohalobacter and Halomonas.";
RL   J. Basic Microbiol. 44:232-240(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 22-36, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=40;
RX   PubMed=23219892; DOI=10.1016/j.ijbiomac.2012.11.029;
RA   Tokunaga H., Furukawa M., Arakawa T., Tokunaga M.;
RT   "Channel forming outer membrane porin protein in halophile: expressed as a
RT   soluble form in Escherichia coli.";
RL   Int. J. Biol. Macromol. 54:44-50(2013).
CC   -!- FUNCTION: Outer membrane porin that allows diffusion of
CC       monosaccharides. Also allows diffusion of disaccharides and
CC       trisaccharides, with reduced diffusion rate.
CC       {ECO:0000269|PubMed:23219892}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000303|PubMed:23219892}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:15162397,
CC       ECO:0000269|PubMed:23219892}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23219892}.
CC   -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR   EMBL; AB244100; BAF96703.1; -; Genomic_DNA.
DR   EMBL; AB183012; BAI63216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9ZM27; -.
DR   SMR; A9ZM27; -.
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:0034220; P:ion transmembrane transport; IEA:InterPro.
DR   CDD; cd00342; gram_neg_porins; 1.
DR   Gene3D; 2.40.160.10; -; 1.
DR   InterPro; IPR033900; Gram_neg_porin_domain.
DR   InterPro; IPR023614; Porin_dom_sf.
DR   InterPro; IPR001702; Porin_Gram-ve.
DR   Pfam; PF13609; Porin_4; 1.
DR   PRINTS; PR00182; ECOLNEIPORIN.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Ion transport; Membrane;
KW   Porin; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15162397,
FT                   ECO:0000269|PubMed:23219892"
FT   CHAIN           22..366
FT                   /note="Monosaccharide porin"
FT                   /id="PRO_0000431311"
SQ   SEQUENCE   366 AA;  39571 MW;  C2F442196DCE193F CRC64;
     MKKTLLATAI AGAMAASGAQ AATVYNQDGT KLDIYGNVQI GFRNIEAEND NGNIETQNDV
     FDNGSTIGFA AEHVIYDGLT GYMKIEFDDF KADEMKTAGR DAGDTAYVGL KGNFGDVKLG
     SYDTLMDDWI QDPITNNEYF DVSDTSGSGS SVVAVGGEVE TDQLTYVSPS FNGLELAIGT
     QYKGDMEEEN VTSRGNASVF GGAKYTAGNF SVAATYDNLD NYEVTQTGVD NKQEFGDRYG
     VTGQYQWNSL RVALKYERFD SDLDNVDSVN FYGLGARYGY GYGDIYGAYQ YVDVGGDTFG
     NVVDDATSGD SPSDTASDRG DDTYNEFIIG GTYNISDAMY TWVEAAFYDR EDDEGDGVAA
     GVTYMF