ID   HLYDP_ECOLX             Reviewed;         478 AA.
AC   P06739;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Hemolysin secretion protein D, plasmid;
GN   Name=hlyD;
OS   Escherichia coli.
OG   Plasmid IncI2 pHLY152.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hess J., Wels W., Vogel M., Goebel W.;
RT   "Nucleotide sequence of a plasmid-encoded hemolysin determinant and its
RT   comparison with a corresponding chromosomal hemolysin sequence.";
RL   FEMS Microbiol. Lett. 34:1-11(1986).
RN   [2]
RP   TOPOLOGY.
RX   PubMed=1495479; DOI=10.1007/bf00272357;
RA   Schuelein R., Gentschev I., Mollenkopf H.-J., Goebel W.;
RT   "A topological model for the haemolysin translocator protein HlyD.";
RL   Mol. Gen. Genet. 234:155-163(1992).
CC   -!- FUNCTION: Involved in the transport of hemolysin A.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; M14107; AAA98235.1; -; Genomic_DNA.
DR   PIR; S10058; S10058.
DR   AlphaFoldDB; P06739; -.
DR   SMR; P06739; -.
DR   DIP; DIP-28121N; -.
DR   TCDB; 8.A.1.3.1; the membrane fusion protein (mfp) family.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   InterPro; IPR006144; Secretion_HlyD_CS.
DR   InterPro; IPR010129; T1SS_HlyD.
DR   TIGRFAMs; TIGR01843; type_I_hlyD; 1.
DR   PROSITE; PS00543; HLYD_FAMILY; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Cytolysis; Hemolysis; Membrane;
KW   Plasmid; Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..478
FT                   /note="Hemolysin secretion protein D, plasmid"
FT                   /id="PRO_0000201874"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:1495479"
FT   TRANSMEM        60..80
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        81..478
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:1495479"
SQ   SEQUENCE   478 AA;  54541 MW;  D286252A35EE3DAC CRC64;
     MKTWLMGFSE FLLRYKLVWS ETWKIRKQLD TPVREKDENE FLPAHLELIE TPVSRRPRLV
     AYFIMGFLVI AFILSVLGQV EIVATANGKL THSGRSKEIK PIENSIVKEI IVKEGESVRK
     GDVLLKLTAL GAEADTLKTQ SSLLQARLEQ TRYQILSRSI ELNKLPELKL PDEPYFQNVS
     EEEVLRLTSL IKEQFSTWQN QKYQKELNLD KKRAERLTVL ARINRYENLS RVEKSRLDDF
     SSLLHKQAIA KHAVLEQENK YVEAVNELRV YKSQLEQIES EILSAKEEYQ LVTQLFKNEI
     LDKLRQTTDN IGLLTLELAK NEERQQASVI RAPVSVKVQQ LKVHTEGGVV TTAETLMVIV
     PEDDTLEVTA LVQNKDIGFI NVGQNAIIKV EAFPYTRYGY LVGKVKNINL DAIEDQRLGL
     VFNVIISIEE NCLSTGNKNI PLSSGMAVTA EIKTGMRSVI SYLLSPLEES VTESLRER