ID D4I1P5_ERWAC Unreviewed; 229 AA.
AC D4I1P5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Surface presentation of antigens protein SpaP {ECO:0000313|EMBL:CBA20536.1};
GN Name=spaP3 {ECO:0000313|EMBL:CBA20536.1};
GN OrderedLocusNames=EAMY_1586 {ECO:0000313|EMBL:CBA20536.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA20536.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA20536.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FliP/MopC/SpaP family.
CC {ECO:0000256|ARBA:ARBA00006257, ECO:0000256|RuleBase:RU362070}.
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DR EMBL; FN434113; CBA20536.1; -; Genomic_DNA.
DR AlphaFoldDB; D4I1P5; -.
DR STRING; 665029.EAMY_1586; -.
DR KEGG; eam:EAMY_1586; -.
DR eggNOG; COG4790; Bacteria.
DR HOGENOM; CLU_042028_2_0_6; -.
DR Proteomes; UP000001841; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:UniProtKB-UniRule.
DR InterPro; IPR005838; T3SS_IM_P.
DR InterPro; IPR005773; T3SS_YscR-like.
DR NCBIfam; TIGR01102; yscR; 1.
DR PANTHER; PTHR30587; FLAGELLAR BIOSYNTHETIC PROTEIN FLIP; 1.
DR PANTHER; PTHR30587:SF2; SURFACE PRESENTATION OF ANTIGENS PROTEIN SPAP; 1.
DR Pfam; PF00813; FliP; 1.
DR PRINTS; PR01302; TYPE3IMPPROT.
DR PROSITE; PS01061; FLIP_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362070};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362070};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362070};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362070}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362070"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362070"
FT TRANSMEM 167..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362070"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362070"
SQ SEQUENCE 229 AA; 25908 MW; 7967F2C828AF8B7F CRC64;
MIWISTMLNN DISLIAVLSF FTLLPFIIAG GTCFIKFSIV LVMMRNALGI QQVPSNLTLN
GISLILTAFI MMPVCQRIID DVETRHIDFN QSSAFSQFVN DGLDGYREYL VHYSDHDLIH
FFNKVQQRNN DDNVANTFEH ELTRLPLMTL MPAYALSEIQ SAFRIAFYIY IPFVVIDMVV
SSILLALGMM MMSPVTISIP IKLILFVAMD GWSLLTKGLI AQYAELMTS
//