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HLY1_AERHH
ID   HLY1_AERHH              Reviewed;         621 AA.
AC   P55870; A0KIE9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Hemolysin ahh1;
DE   Flags: Precursor;
GN   Name=ahh1; OrderedLocusNames=AHA_1512;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-621.
RX   PubMed=1800890; DOI=10.1016/0882-4010(91)90049-g;
RA   Hirono I., Aoki T.;
RT   "Nucleotide sequence and expression of an extracellular hemolysin gene of
RT   Aeromonas hydrophila.";
RL   Microb. Pathog. 11:189-197(1991).
CC   -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC       membranes and cause cell rupture by mechanisms not clearly defined.
CC   -!- SIMILARITY: Belongs to the HlyA hemolysin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000462; ABK36614.1; -; Genomic_DNA.
DR   PIR; A61372; A61372.
DR   RefSeq; WP_011705409.1; NC_008570.1.
DR   RefSeq; YP_856050.1; NC_008570.1.
DR   AlphaFoldDB; P55870; -.
DR   SMR; P55870; -.
DR   STRING; 380703.AHA_1512; -.
DR   TCDB; 1.C.14.1.2; the cytohemolysin (chl) family.
DR   PRIDE; P55870; -.
DR   EnsemblBacteria; ABK36614; ABK36614; AHA_1512.
DR   KEGG; aha:AHA_1512; -.
DR   PATRIC; fig|380703.7.peg.1525; -.
DR   eggNOG; ENOG502ZBG7; Bacteria.
DR   HOGENOM; CLU_439829_0_0_6; -.
DR   OMA; HVAFYLN; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 3.30.110.130; -; 1.
DR   Gene3D; 6.20.40.20; -; 1.
DR   InterPro; IPR022220; Hemolysin_N.
DR   InterPro; IPR043080; Hemolysin_N_sf.
DR   InterPro; IPR044883; Hemolysin_pre-stem_dom_sf.
DR   InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR   InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF12563; Hemolysin_N; 1.
DR   Pfam; PF07968; Leukocidin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   SUPFAM; SSF56959; SSF56959; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Hemolysis; Lectin; Reference proteome; Signal; Toxin; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..621
FT                   /note="Hemolysin ahh1"
FT                   /id="PRO_0000013366"
FT   DOMAIN          491..610
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   CONFLICT        64
FT                   /note="R -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="S -> I (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="T -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="V -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157..158
FT                   /note="KR -> NG (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="G -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="T -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289..290
FT                   /note="SI -> TT (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="T -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="C -> F (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527
FT                   /note="F -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="Q -> E (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="R -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583
FT                   /note="G -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  68907 MW;  99C8E4BD6055381D CRC64;
     MKNKKPRKFI TQAPTLSLLA LALLAGSVQA EDIGERTDQG TAMLASLQSE QGLIYLNADV
     WLKRQGATPL MTRDQLRERV LARGERLFID FSAVTDQSER QQTRKAMEQL AGISFDADWV
     LVSGYKGELL FTPLGGVDDP AFYQVMERVE SLEGQGKRHK RSLTQPPAAE AGLPHVAFYL
     NVNRKISDAE CTFPRSRTWS RGDRLFCDSP NISLVYRVNL ERSLQFGNTG SATPDAKIVR
     ISLDEESAGA GIQLNEDLTW SENIADYLLL DGWARDYATD AIAQDYRFSI EASNTKAAVL
     KSLPTNLNSK YEHREISGFE VGVTGGVEVN KDGPKAKLEA SAKFSQQRQL AYNTQDYRVE
     RSAPSAQKVS FSWVRDQYAT AESLLSSKTA TVWGMGYDVD HNRIQPLSYK GFVPNLDVIY
     KAAPDETGST EFKIDSSVNI RPIYTGIYKH YYVVGAHVSF QGFEDTDKRR RVTASTSFKV
     DWNHPVFTGG RPVNLQLGGF DNRCLSADAN HGLSAVTCDE TSAAQSFIYD QYGRYVSAQD
     TRRCLDGNNL GQLQSCSLSL GQRWEWKADS DALSNLSAHQ LLGHDKQSGA LGLYDENGNP
     QNVSVRTLTS YTRIFGPPAS H
 
 
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