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Database: UniProt
Entry: A0A0W0Z4K4_LEGSP
LinkDB: A0A0W0Z4K4_LEGSP
Original site: A0A0W0Z4K4_LEGSP 
ID   A0A0W0Z4K4_LEGSP        Unreviewed;       441 AA.
AC   A0A0W0Z4K4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   Name=lssD_1 {ECO:0000313|EMBL:KTD64080.1};
GN   ORFNames=Lspi_1599 {ECO:0000313|EMBL:KTD64080.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD64080.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD64080.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD64080.1,
RC   ECO:0000313|Proteomes:UP000054877};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD64080.1}.
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DR   EMBL; LNYX01000014; KTD64080.1; -; Genomic_DNA.
DR   RefSeq; WP_058483509.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0Z4K4; -.
DR   STRING; 452.Lspi_1599; -.
DR   PATRIC; fig|452.5.peg.1758; -.
DR   Proteomes; UP000054877; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR010129; T1SS_HlyD.
DR   NCBIfam; TIGR01843; type_I_hlyD; 1.
DR   PANTHER; PTHR30386:SF17; ALKALINE PROTEASE SECRETION PROTEIN APRE; 1.
DR   PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   PRINTS; PR01490; RTXTOXIND.
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|RuleBase:RU365093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054877};
KW   Transmembrane {ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        17..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   COILED          165..199
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          253..294
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   441 AA;  49766 MW;  242E5928501A27EB CRC64;
     MDNGNPHKLP ETSESPIITS ILIFGFIILI VFVGGFLLWS MLFRLDAAAV APGKLMVQNV
     RKTVQHMEGG IIKKIYIDEG SAVKANTPLI KLDDTQAKAS VDLLQGQVYE NLASESRIFA
     ELNNEKTIDY PEELLQKATN PKVKKIISGQ NKLFTANTRS YEGQIKVLNE RIEEFHHEIK
     SLEAQVDSGT EQLSLINEEI KAVEYLEARK LIDKPRLLAL RREAARLTGN RGEHLGLVAK
     AHQAISETKS QIYTLMESRR RDLLQNLREI QQKLADLQEK LKAAQDVLQR TLIAAPLTGT
     VIGLKKHTVG GVITPGQDIL DIIPSEDQLI VEAEVDPLDI DIVRPGLTAK VRLSAYKQRT
     TPFIEGKVKL VSADVFEDQV TKKQYYKVHI LLDKKDLQQL KHIHLYPGMP VQVMIIVEKR
     TAFDYFITPI QDSFERAFHE Q
//
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