ID HLYBC_ECOLX Reviewed; 707 AA.
AC P10089;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
GN Name=hlyB;
OS Escherichia coli.
OC Bacteria; Pseudomonadota; 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).
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.
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}.
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DR EMBL; M10133; AAA23976.1; -; Genomic_DNA.
DR RefSeq; WP_021525012.1; NZ_SAGY01000029.1.
DR AlphaFoldDB; P10089; -.
DR BMRB; P10089; -.
DR SMR; P10089; -.
DR DIP; DIP-16931N; -.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd18588; ABC_6TM_CyaB_HlyB_like; 1.
DR CDD; cd03252; ABCC_Hemolysin; 1.
DR CDD; cd02417; Peptidase_C39_likeA; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01846; type_I_sec_HlyB; 1.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 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; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..707
FT /note="Alpha-hemolysin translocation ATP-binding protein
FT HlyB"
FT /id="PRO_0000092372"
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"
SQ SEQUENCE 707 AA; 79464 MW; 21009CB45E59437E CRC64;
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV
KKTIDRLNFI SLPALVWRED GCHFILTKVS KEANRYLIFD LEQRNPRVLE QSEFEALYQG
HIILIASRSS VTGKLAKFDF TWFIPAIIKY RKIFIETLVV 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 EHVIMRNMHK ICKGRTVIII
AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD
//
