HLYD_MANHA
ID HLYD_MANHA Reviewed; 478 AA.
AC P16534;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Leukotoxin secretion protein D;
GN Name=lktD;
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A1;
RX PubMed=3040588; DOI=10.1128/iai.55.9.1987-1996.1987;
RA Lo R.Y.C., Strathdee C.A., Shewen P.E.;
RT "Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica
RT A1.";
RL Infect. Immun. 55:1987-1996(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A1;
RX PubMed=2914876; DOI=10.1128/jb.171.2.916-928.1989;
RA Strathdee C.A., Lo R.Y.C.;
RT "Cloning, nucleotide sequence, and characterization of genes encoding the
RT secretion function of the Pasteurella haemolytica leukotoxin determinant.";
RL J. Bacteriol. 171:916-928(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A1 / PH101;
RX PubMed=2707120; DOI=10.1089/dna.1.1989.8.15;
RA Highlander S.K., Chidambaram M., Engler M.J., Weinstock G.M.;
RT "DNA sequence of the Pasteurella haemolytica leukotoxin gene cluster.";
RL DNA 8:15-28(1989).
CC -!- FUNCTION: Involved in the transport of the Leukotoxin.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; M20730; AAA25531.1; -; Genomic_DNA.
DR EMBL; M24197; AAA25545.1; -; Genomic_DNA.
DR PIR; D30169; D30169.
DR AlphaFoldDB; P16534; -.
DR SMR; P16534; -.
DR STRING; 75985.WC39_13380; -.
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; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR TIGRFAMs; TIGR01843; type_I_hlyD; 1.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytolysis; Hemolysis; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..478
FT /note="Leukotoxin secretion protein D"
FT /id="PRO_0000201876"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..478
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 18
FT /note="T -> I (in Ref. 3; AAA25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> E (in Ref. 3; AAA25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> T (in Ref. 3; AAA25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="F -> L (in Ref. 3; AAA25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..267
FT /note="EL -> AV (in Ref. 3; AAA25545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54761 MW; E2B8B5FF5AF988C1 CRC64;
MKIWLSGIYE FFLRYKNTWA EVWKIRKELD HPNRKKDESE FLPAHLDLIE TPVSKKPRLI
AYLIMLFLVV AIVLASVSKV EIVATAPGKL TFSGRSKEIK PIENAIVQEI FVKDGQFVEK
GQLLVSLTAL GSDADIKKTM ASLSLAKLEN YRYQTLLTAI EKESLPVIDL SRTEFKDSSE
EDRLRIKHLI EEQYTTWQKQ KTQKTLAYKR KEAEKQTIFA YVRKYEGATR IEQEKFKDFK
ALYKQKSLSK HELLAQENKL IEAQNELAVY RSKLNELEND LLNVKEELEL ITQFFKSDVL
EKLKQHIENE RQLRLELEKN NQRRQASMIR APVSGTVQQL KIHTIGGVVT TAETLMIIVP
EDDVLEATAL VPNKDIGFVA AGQEVIIKVE TFPYTRYGYL TGRIKHISPD AIEQPNVGLV
FNATIAIDRK NLTSPDGRKI DLSSGMTITA EIKTGERSVM SYLLSPLEES VTESLRER