ID   AMSH_ERWAM              Reviewed;         377 AA.
AC   Q46629;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Amylovoran export outer membrane protein AmsH;
DE   Flags: Precursor;
GN   Name=amsH;
OS   Erwinia amylovora (Fire blight bacteria).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EA1/79;
RX   PubMed=7596293; DOI=10.1111/j.1365-2958.1995.tb02361.x;
RA   Bugert P., Geider K.;
RT   "Molecular analysis of the ams operon required for exopolysaccharide
RT   synthesis of Erwinia amylovora.";
RL   Mol. Microbiol. 15:917-933(1995).
RN   [2]
RP   SEQUENCE REVISION TO 14; 221; 235 AND 311.
RA   Geider K.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of amylovoran which functions as
CC       a virulence factor. Might be involved in the translocation of
CC       polysaccharides across the outer membrane.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BexD/CtrA/VexA family. {ECO:0000305}.
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DR   EMBL; X77921; CAA54880.2; -; Genomic_DNA.
DR   PIR; S61892; S61892.
DR   AlphaFoldDB; Q46629; -.
DR   SMR; Q46629; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003715; Poly_export.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   InterPro; IPR040716; Wza_C.
DR   Pfam; PF02563; Poly_export; 1.
DR   Pfam; PF10531; SLBB; 2.
DR   Pfam; PF18412; Wza_C; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Ion transport; Lipoprotein; Membrane; Palmitate;
KW   Polysaccharide transport; Porin; Signal; Sugar transport; Transmembrane;
KW   Transmembrane beta strand; Transport; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..377
FT                   /note="Amylovoran export outer membrane protein AmsH"
FT                   /id="PRO_0000025215"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   377 AA;  41530 MW;  62AFD85FEC4D9623 CRC64;
     MIIIKTKLIP LMVSAALLSG CTIVPGNHLS TMGKDVVEQQ DSDFDIDKYV NIFPLTPSLV
     ERMKPKPVVA QANATLQREL QNYEYRIGVG DVLMVTVWDH PELTTPAGQY RSASDTGNWV
     HSDGTIFYPY IGRVRVAGHT VQETRDEIAS RLSKYVESPQ VDVNVASFKS QKTYVTGEVT
     TSGQQAITNV PLTILDAINA AGGLTATADW RNVVLTHDGR EQPVSLQALM QNGDLSQNHL
     LYPGDILYVP RNDDLKVFVM GEVKQQATLK MDRSGMTLSE ALGSAQGMDQ SVADATGVFV
     IRPVKGANRS KIANIYQLNT KDAAAMVMGT EFRLEPYDIV YVTSTPLTRW NRVISQLVPT
     ISGVYDATRN VQTIHKW