HLYB3_ECOLX
ID HLYB3_ECOLX Reviewed; 707 AA.
AC Q47258;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
GN Name=hlyB;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LE2001 / UPEC;
RX PubMed=1371277; DOI=10.1016/s0021-9258(19)50591-9;
RA Juranka P., Zhang F., Kulpa J., Endicott J.A., Blight M., Holland I.B.,
RA Ling V.;
RT "Characterization of the hemolysin transporter, HlyB, using an epitope
RT insertion.";
RL J. Biol. Chem. 267:3764-3770(1992).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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. These channel is involved in type 1 secretion system (By
CC similarity). {ECO:0000250}.
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 they are
CC presumed to be without peptidase activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M81823; AAA23978.1; -; Genomic_DNA.
DR PIR; A42255; LEECB.
DR RefSeq; WP_000376543.1; NZ_WIKQ01000030.1.
DR PDB; 3ZUA; NMR; -; A=2-137.
DR PDBsum; 3ZUA; -.
DR AlphaFoldDB; Q47258; -.
DR BMRB; Q47258; -.
DR SMR; Q47258; -.
DR OMA; ERQRMTI; -.
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:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..707
FT /note="Alpha-hemolysin translocation ATP-binding protein
FT HlyB"
FT /id="PRO_0000092373"
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 HELIX 9..20
FT /evidence="ECO:0007829|PDB:3ZUA"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:3ZUA"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:3ZUA"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3ZUA"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3ZUA"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:3ZUA"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3ZUA"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3ZUA"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:3ZUA"
SQ SEQUENCE 707 AA; 79529 MW; E709E59F21BDA853 CRC64;
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV
KKTIDRLNFI SLPALVWRED GRHFILTKVS KEANRYLIFD LEQRNPRVLE QSEFEALYQG
HIILIASRSS VAGKLAKFDF TWFIPAIIKY RRIFIETLVV SVFLQLFALI TPLFFQVVMD
KVLVHRGFST LNVITVALSV VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI
SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL
AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTESYHGKLA LPEINGDITF RNIRFRYKPD
SPVILDNINL SIKQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHIIMRNMHK ICKGRTVIII
AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD
