HLYDC_ECOLX
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