HLYBP_ECOLX
ID HLYBP_ECOLX Reviewed; 707 AA.
AC P08716;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
GN Name=hlyB;
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 REQUIREMENT OF TOLC FOR HEMOLYSIN EXPORT.
RX PubMed=2112747; DOI=10.1073/pnas.87.12.4776;
RA Wandersman C., Delepelaire P.;
RT "TolC, an Escherichia coli outer membrane protein required for hemolysin
RT secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4776-4780(1990).
RN [3]
RP TOPOLOGY.
RX PubMed=1552901; DOI=10.1007/bf00299135;
RA Gentschev I., Goebel W.;
RT "Topological and functional studies on HlyB of Escherichia coli.";
RL Mol. Gen. Genet. 232:40-48(1992).
RN [4]
RP TOPOLOGY.
RX PubMed=1994034; DOI=10.1016/0022-2836(91)90748-u;
RA Wang R.C., Seror S.J., Blight M., Pratt J.M., Broome-Smith J.K.,
RA Holland I.B.;
RT "Analysis of the membrane organization of an Escherichia coli protein
RT translocator, HlyB, a member of a large family of prokaryote and eukaryote
RT surface transport proteins.";
RL J. Mol. Biol. 217:441-454(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 467-707.
RX PubMed=12823972; DOI=10.1016/s0022-2836(03)00592-8;
RA Schmitt L., Benabdelhak H., Blight M.A., Holland I.B., Stubbs M.T.;
RT "Crystal structure of the nucleotide-binding domain of the ABC-transporter
RT haemolysin B: identification of a variable region within ABC helical
RT domains.";
RL J. Mol. Biol. 330:333-342(2003).
RN [6]
RP REVIEW.
RX PubMed=3017638; DOI=10.1007/978-3-642-71251-7_10;
RA Mackman N., Nicaud J.-M., Gray L., Holland I.B.;
RT "Secretion of haemolysin by Escherichia coli.";
RL Curr. Top. Microbiol. Immunol. 125:159-181(1986).
RN [7]
RP REVIEW.
RA Holland I.B., Benabdelhak H., Young J., de Lima Pimenta A., Schmitt L.,
RA Blight M.A.;
RT "Bacterial ABC transporters involved in protein translocation.";
RL (In) Holland I.B., Cole S.P.C., Kuchler K., Higgins C.F. (eds.);
RL ABC proteins from bacteria to man, pp.209-241, Academic Press, San Diego.
RL (2003).
CC -!- FUNCTION: Part of the ABC transporter complex HlyBD involved in
CC hemolysin export. Transmembrane domains (TMD) form a pore in the inner
CC membrane and the ATP-binding domain (NBD) is responsible for energy
CC generation.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: In HlyB the peptidase C39 domain, the ATP-binding domain (NBD)
CC and the transmembrane domain (TMD) are fused.
CC -!- MISCELLANEOUS: The complex HlyBD-TolC (OMF) forms a single transport
CC channel across the two membranes, allowing direct export of alpha-
CC hemolysin. This channel is involved in type 1 secretion system.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC -!- CAUTION: Tyr-9 is present instead of the conserved Cys which is
CC expected to be the active site residue of peptidase C39. Thus this
CC protein is presumed to be without peptidase activity. {ECO:0000305}.
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DR EMBL; M14107; AAA98234.1; -; Genomic_DNA.
DR PIR; S10057; S10057.
DR PDB; 1MT0; X-ray; 2.60 A; A=467-707.
DR PDB; 1XEF; X-ray; 2.50 A; A/B/C/D=467-707.
DR PDB; 2FF7; X-ray; 1.60 A; A=467-707.
DR PDB; 2FFA; X-ray; 1.70 A; A=467-707.
DR PDB; 2FFB; X-ray; 1.90 A; A=467-707.
DR PDB; 2FGJ; X-ray; 2.60 A; A/B/C/D=467-707.
DR PDB; 2FGK; X-ray; 2.70 A; A/B/C/D=467-707.
DR PDB; 2PMK; X-ray; 1.60 A; A=467-707.
DR PDB; 3B5J; X-ray; 2.00 A; A=467-707.
DR PDBsum; 1MT0; -.
DR PDBsum; 1XEF; -.
DR PDBsum; 2FF7; -.
DR PDBsum; 2FFA; -.
DR PDBsum; 2FFB; -.
DR PDBsum; 2FGJ; -.
DR PDBsum; 2FGK; -.
DR PDBsum; 2PMK; -.
DR PDBsum; 3B5J; -.
DR AlphaFoldDB; P08716; -.
DR SMR; P08716; -.
DR DIP; DIP-28120N; -.
DR TCDB; 3.A.1.109.1; the atp-binding cassette (abc) superfamily.
DR EvolutionaryTrace; P08716; -.
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:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:CAFA.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0032940; P:secretion by cell; IDA:CAFA.
DR GO; GO:1901998; P:toxin transport; IDA:CAFA.
DR CDD; cd02417; Peptidase_C39_likeA; 1.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR010132; ATPase_T1SS_HlyB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039395; Peptidase_C39-like_A.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW Membrane; Nucleotide-binding; Plasmid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..707
FT /note="Alpha-hemolysin translocation ATP-binding protein
FT HlyB"
FT /id="PRO_0000092371"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 3..125
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 154..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 468..703
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 467..478
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 483..493
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 508..515
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:2FF7"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 538..544
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:1XEF"
FT HELIX 559..563
FT /evidence="ECO:0007829|PDB:2FF7"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 585..589
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:1XEF"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:3B5J"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 608..620
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:2FF7"
FT TURN 632..635
FT /evidence="ECO:0007829|PDB:1MT0"
FT HELIX 638..652
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 655..660
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 664..667
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 670..677
FT /evidence="ECO:0007829|PDB:2FF7"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 687..691
FT /evidence="ECO:0007829|PDB:2FF7"
FT HELIX 697..705
FT /evidence="ECO:0007829|PDB:2FF7"
SQ SEQUENCE 707 AA; 79673 MW; 412A3EB64A3CFFBA CRC64;
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV
KKTIDRLNFI FLPALVWRED GRHFILTKIS KEVNRYLIFD LEQRNPRVLE QSEFEALYQG
HIILITSRSS VTGKLAKFDF TWFIPAIIKY RRIFIETLVV SVFLQLFALI TPLFFQVVMD
KVLVHRGFST LNVITVALSV VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI
SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLLFSL IFFAVMWYYS PKLTLVILFS
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL
AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTESYHGKLT LPEINGDITF RNIRFRYKPD
SPVILDNINL SIKQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHVIMRNMHK ICKGRTVIII
AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD
