RTX1B_ACTPL
ID RTX1B_ACTPL Reviewed; 707 AA.
AC P26760;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Toxin RTX-I translocation ATP-binding protein;
DE AltName: Full=APX-IB;
DE AltName: Full=Cytolysin IB;
DE Short=CLY-IB;
DE AltName: Full=HLY-IB;
DE AltName: Full=RTX-I toxin determinant B;
GN Name=apxIB; Synonyms=appB, clyIB, hlyIB;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 5;
RX PubMed=1860823; DOI=10.1128/jb.173.16.5151-5158.1991;
RA Chang Y.-F., Young R., Struck D.K.;
RT "The Actinobacillus pleuropneumoniae hemolysin determinant: unlinked appCA
RT and appBD loci flanked by pseudogenes.";
RL J. Bacteriol. 173:5151-5158(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate CVI 13261 / Serotype 9;
RX PubMed=1937809; DOI=10.1128/iai.59.12.4497-4504.1991;
RA Smits M.A., Briaire J., Jansen R., Smith H.E., Kamp E.M., Gielkens A.L.J.;
RT "Cytolysins of Actinobacillus pleuropneumoniae serotype 9.";
RL Infect. Immun. 59:4497-4504(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=8181764; DOI=10.1016/0378-1119(94)90361-1;
RA Frey J., Haldimann A., Nicolet J., Boffini A., Prentki P.;
RT "Sequence analysis and transcription of the apxI operon (hemolysin I) from
RT Actinobacillus pleuropneumoniae.";
RL Gene 142:97-102(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-326, AND CHARACTERIZATION IN VIVO.
RC STRAIN=CM5 / Serotype 1;
RX PubMed=7830567; DOI=10.1111/j.1365-2958.1994.tb01282.x;
RA Tascon R.I., Vazquez-Boland J.A., Gutierrez-Martin C.B.,
RA Rodriguez-Barbosa I., Rodriguez-Ferri E.F.;
RT "The RTX haemolysins ApxI and ApxII are major virulence factors of the
RT swine pathogen Actinobacillus pleuropneumoniae: evidence from mutational
RT analysis.";
RL Mol. Microbiol. 14:207-216(1994).
CC -!- FUNCTION: Involved in the transport of the toxin RTX-I as well as that
CC of RTX-II.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: The sequence shown is that of serotype 9.
CC -!- MISCELLANEOUS: In strain CM15 (serotype 1), disruption of this gene
CC prevents production of both RTX-I and RTX-II toxin, and no hemolytic
CC activity in mice or pigs.
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; M65808; AAB00966.1; -; Genomic_DNA.
DR EMBL; X61112; CAA43425.1; -; Genomic_DNA.
DR EMBL; X68595; CAA48587.1; -; Genomic_DNA.
DR PIR; D43599; D43599.
DR AlphaFoldDB; P26760; -.
DR SMR; P26760; -.
DR STRING; 228399.appser1_15230; -.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytolysis; Hemolysis; Membrane;
KW Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..707
FT /note="Toxin RTX-I translocation ATP-binding protein"
FT /id="PRO_0000092390"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
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 TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1..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 VARIANT 110..112
FT /note="EQA -> KQT (in strain: Serotype 5)"
FT VARIANT 328
FT /note="D -> H (in strain: Serotype 5)"
FT VARIANT 517
FT /note="R -> V (in strain: Serotype 5)"
FT VARIANT 556
FT /note="N -> G (in strain: Serotype 5)"
FT VARIANT 609..611
FT /note="GQR -> RAT (in strain: S 4074 / Serotype 1)"
FT VARIANT 611..612
FT /note="RQ -> PN (in strain: Serotype 5)"
FT VARIANT 671..672
FT /note="DR -> AS (in strain: Serotype 5)"
FT VARIANT 692
FT /note="A -> R (in strain: Serotype 5)"
SQ SEQUENCE 707 AA; 79664 MW; 34A4339C57340DF9 CRC64;
MDFYREEDYG LYALTILAQY HNIAVNPEEL KHKFDLEGKG LDLTAWLLAA KSLELKAKQV
KKAIDRLAFI ALPALVWRED GKHFILTKID NEAKKYLIFD LETHNPRILE QAEFESLYQG
KLILVASRAS IVGKLAKFDF TWFIPAVIKY RKIFIETLIV SIFLQIFALI TPLFFQVVMD
KVLVHRGFST LNVITVALAI VVLFEIVLNG LRTYIFAHST SRIDVELGAR LFRHLLALPI
SYFENRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLMFSF IFFAVMWYYS PKLTLVILGS
LPFYMGWSIF ISPILRRRLD EKFARGADNQ SFLVESVTAI NTIKALAVTP QMTNTWDKQL
ASYVSAGFRV TTLATIGQQG VQFIQKVVMV ITLWLGAHLV ISGDLSIGQL IAFNMLSGQV
IAPVIRLAQL WQDFQQVGIS VTRLGDVLNS PTESYQGKLA LPEIKGDITF RNIRFRYKPD
APVILNDVNL SIQQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSIR DNIALADPGM PMEKIVHAAK LAGAHEFISE LREGYNTIVG
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHIIMRNMHQ ICKGRTVIII
AHRLSTVKNA DRIIVMEKGQ IVEQGKHKEL LADPNGLYHY LHQLQSE
