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 02-NOV-2016, entry version 66.
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
CC functions as a virulence factor. Might be involved in the
CC translocation of polysaccharides across the outer membrane.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BexD/CtrA/VexA family. {ECO:0000305}.
DR EMBL; X77921; CAA54880.2; -; Genomic_DNA.
DR PIR; S61892; S61892.
DR STRING; 665029.EAMY_2252; -.
DR PRIDE; Q46629; -.
DR eggNOG; ENOG4105DAY; Bacteria.
DR eggNOG; COG1596; LUCA.
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 GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR003715; Poly_export.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF02563; Poly_export; 1.
DR Pfam; PF10531; SLBB; 2.
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;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT CHAIN 21 377 Amylovoran export outer membrane protein
FT AmsH.
FT /FTId=PRO_0000025215.
FT LIPID 21 21 N-palmitoyl cysteine.
FT {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT LIPID 21 21 S-diacylglycerol cysteine.
FT {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 256 306 ipfam:SLBB [T]
FT MYHIT 81 165 ipfam:Poly_export [T]
FT MYHIT 173 222 ipfam:SLBB [T]
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
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