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Database: UniProt
Entry: A0A083ZWF8_9GAMM
LinkDB: A0A083ZWF8_9GAMM
Original site: A0A083ZWF8_9GAMM 
ID   A0A083ZWF8_9GAMM        Unreviewed;       456 AA.
AC   A0A083ZWF8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   Name=prsE {ECO:0000313|EMBL:KEY57387.1};
GN   ORFNames=SRDD_37570 {ECO:0000313|EMBL:KEY57387.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY57387.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY57387.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY57387.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(2014).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU365093}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU365093}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|RuleBase:RU365093}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEY57387.1}.
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DR   EMBL; AYKS02000092; KEY57387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A083ZWF8; -.
DR   STRING; 1410619.SRDD_37570; -.
DR   eggNOG; COG0845; Bacteria.
DR   Proteomes; UP000017810; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   InterPro; IPR006144; Secretion_HlyD_CS.
DR   InterPro; IPR010129; T1SS_HlyD.
DR   NCBIfam; TIGR01843; type_I_hlyD; 1.
DR   PANTHER; PTHR30386:SF25; MANNURONAN SYNTHASE; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   PRINTS; PR01490; RTXTOXIND.
DR   PROSITE; PS00543; HLYD_FAMILY; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365093};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU365093}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        82..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   DOMAIN          121..154
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          262..289
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        37..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50131 MW;  E136B4962DC6CB07 CRC64;
     MNKDDVALAG PDNADYSNNG DGTIADNEAK IKTVNQPDKV NSKKKKDGNN LQHTGKIEPD
     DLHFMNDLQA ALISQKTPFS MIMLYLILIV LVVALVWAHF AKVEEVTRGE GKIIPASHEQ
     VIQSLEGGIL AEMNVREGDI VEKGQVLLKM DPTRAGASYG ESLSKVLALK GTIARLRAQA
     YDTELVFPPE VQADPSIIED ETKAHNAQLK TLNDSVAALK KSLSLAENEV SLSAPLAQKG
     LMSDVEILRL RRQANEFQLQ IVDRINRFRS EANNELNKAE SELAQTQEVL RGRQDVMQRT
     TIVAPVRGTV NNIHTTTIGG VIAQGAEIMT IIPLEDNLLV EAKIKPADVA FIRPGLPATV
     KVTAYDYAIY GGLSGVVEHL SSDTLVDEEK ARAGRGDSTY YRVYVRTDQA ALHMKDKTFP
     IMPGMVADVE IRTGEKTILS YILKPVLKAR EAFRER
//
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