ID   HLYDC_ECOLX             Reviewed;         478 AA.
AC   P09986;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Hemolysin secretion protein D, chromosomal;
GN   Name=hlyD;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J96 / Serotype O4;
RX   PubMed=3891743; DOI=10.1128/jb.163.1.94-105.1985;
RA   Felmlee T., Pellett S., Welch R.A.;
RT   "Nucleotide sequence of an Escherichia coli chromosomal hemolysin.";
RL   J. Bacteriol. 163:94-105(1985).
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; M10133; AAA23977.1; -; Genomic_DNA.
DR   PIR; D24433; LEECD.
DR   RefSeq; WP_001528401.1; NZ_VOTV01000033.1.
DR   PDB; 5C21; X-ray; 2.50 A; A/B=96-372.
DR   PDB; 5C22; X-ray; 2.30 A; A/B/C/D=96-372.
DR   PDBsum; 5C21; -.
DR   PDBsum; 5C22; -.
DR   AlphaFoldDB; P09986; -.
DR   SMR; P09986; -.
DR   DIP; DIP-16930N; -.
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:0019534; F:toxin transmembrane transporter activity; IDA:CAFA.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   GO; GO:0032940; P:secretion by cell; IDA:CAFA.
DR   GO; GO:1901998; P:toxin transport; IDA:CAFA.
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   3D-structure; Cell inner membrane; Cell membrane; Cytolysis; Hemolysis;
KW   Membrane; Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..478
FT                   /note="Hemolysin secretion protein D, chromosomal"
FT                   /id="PRO_0000201873"
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"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   HELIX           132..162
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   HELIX           181..241
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   TURN            244..247
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   HELIX           251..325
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   STRAND          328..331
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   STRAND          336..340
FT                   /evidence="ECO:0007829|PDB:5C22"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:5C21"
FT   STRAND          357..360
FT                   /evidence="ECO:0007829|PDB:5C22"
SQ   SEQUENCE   478 AA;  54591 MW;  9E9EDC42EC8D8089 CRC64;
     MKTWLMGFSE FLLRYKLVWS ETWKIRKQLD TPVREKDENE FLPAHLELIE TPVSRRPRLV
     AYFIMGFLVI AFILSVLGQV EIVATANGKL TLSGRSKEIK PIENSIVKEI IVKEGESVRK
     GDVLLKLTAL GAEADTLKTQ SSLLQARLEQ IRYQILSRSI ELNKLPELKL PDEPYFQNVS
     EEEVLRLTSL IKEQFSTWQN QKYQKELNLD KKRAERLTIL ARINRYENVS RVEKSRLDDF
     RSLLHKQAIA KHAVLEQENK YVEAANELRV YKSQLEQIES EILSAKEEYQ LVTQLFKNEI
     LDKLRQTTDS IELLTLELEK NEERQQASVI RAPVSGKVQQ LKVHTEGGVV TTAETLMVIV
     PEDDTLEVTA LVQNKDIGFI NVGQNAIIKV EAFPYTRYGY LVGKVKNINL DAIEDQKLGL
     VFNVIVSVEE NDLSTGNKHI PLSSGMAVTA EIKTGMRSVI SYLLSPLEES VTESLHER