ID   HLYB_PROVU              Reviewed;         707 AA.
AC   P11599;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
GN   Name=hlyB;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3054490; DOI=10.1007/bf00339631;
RA   Koronakis V., Koronakis E., Hughes C.;
RT   "Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris
RT   and Escherichia coli; site-directed mutagenesis causing impairment of
RT   export function.";
RL   Mol. Gen. Genet. 213:551-555(1988).
CC   -!- FUNCTION: Involved in the export of hemolysin A.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; X12852; CAA31330.1; -; Genomic_DNA.
DR   PIR; S05477; LEEBBV.
DR   AlphaFoldDB; P11599; -.
DR   SMR; P11599; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytolysis; Hemolysis; 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_0000092376"
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        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          2..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;  79940 MW;  6972C5D4EB18204F CRC64;
     MDFHHKNNYG LYALEILAQY HNISINPEEI KHKFDINGVG LDLTSWLLAA KSLELKVKAV
     KKTIERLNFI YLPALVWRED GHHFILTKVN KESNRYLIYD LEQRNPRVLE QAEFEDLYQG
     NIILITSRSS VIGKLAKFDF TWFIPAVIKY RKIFIETLIV SVFLQLFALI TPLFFQVVMD
     KVLVHRGFST LNIITIALAV VAIFEITLSG LRTYIFTHST SRIDVELGAK LFRHLLALPI
     SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSILDLLFSF IFFAVMWYYS PKLTLVILFS
     LPCYATWSIF ISPILRRRLD DKFARNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL
     AGYVAAGFKV TVLATIGQQG IQLIQKAVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
     VAPVIRLAQL WQDFQQVGIS VTRLGDVLNY PTESYQGKLT LPEINGDISF RNIRFRYKPD
     APIILNNINL NIKQGEIIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
     LRRQVGVVLQ DNVLLNRSII DNIALADPGM PVEKVIHAAK LAGAHDFISE LREGYNTIVG
     EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHVIMRNMHK ICQGRTVIII
     AHRLSTVKNA DRIIVMEKGQ IIEQGKHKEL LSDPESLYHY LHQLQSD