ID K0MHQ5_BORPB Unreviewed; 2030 AA.
AC K0MHQ5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Hemolysin {ECO:0000313|EMBL:CCJ51023.1};
GN OrderedLocusNames=BN117_3690 {ECO:0000313|EMBL:CCJ51023.1};
OS Bordetella parapertussis (strain Bpp5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ51023.1, ECO:0000313|Proteomes:UP000008035};
RN [1] {ECO:0000313|EMBL:CCJ51023.1, ECO:0000313|Proteomes:UP000008035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ51023.1,
RC ECO:0000313|Proteomes:UP000008035};
RX PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT "Comparative genomics of the classical Bordetella subspecies: the evolution
RT and exchange of virulence-associated diversity amongst closely related
RT pathogens.";
RL BMC Genomics 13:545-545(2012).
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; HE965803; CCJ51023.1; -; Genomic_DNA.
DR RefSeq; WP_015040403.1; NC_018828.1.
DR RefSeq; YP_006897466.1; NC_018828.1.
DR KEGG; bpar:BN117_3690; -.
DR HOGENOM; CLU_000532_0_0_4; -.
DR Proteomes; UP000008035; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd00198; vWFA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR041690; Cadherin_5.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR047777; LapA-like_RM.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR019960; T1SS_VCA0849.
DR InterPro; IPR010221; VCBS_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR NCBIfam; NF033682; retention_LapA; 1.
DR NCBIfam; TIGR03661; T1SS_VCA0849; 1.
DR NCBIfam; NF012211; tand_rpt_95; 3.
DR NCBIfam; TIGR01965; VCBS_repeat; 4.
DR Pfam; PF17803; Cadherin_4; 2.
DR Pfam; PF17892; Cadherin_5; 2.
DR Pfam; PF05345; He_PIG; 2.
DR Pfam; PF00353; HemolysinCabind; 4.
DR Pfam; PF13519; VWA_2; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00736; CADG; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50268; CADHERIN_2; 2.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
FT DOMAIN 190..292
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 420..513
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1412..1577
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 161..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2030 AA; 208060 MW; 8528380A07987F56 CRC64;
MANSSPAVVT AVTGRAWIRN SDGSLTELHE GSKVPQGSDI VTASGSTVAL PVDGGMPLVI
GEGREVAVTP DLNGGGGDAS EAAVALPTTT DSERLLAALQ DGRDPFDELD PTAAVIGGSG
DSAGSSFVRL AKILESTTPM DLAYPNPGRG EDGVRTFLGG ATAGADDEAA PAPANQAPNA
LDDLGQTRQG QALRGNLMLN DSDPDGDPLT VVSVNGRPMT SGGLTLPGSG GGTFTVQPDG
SYTFVPGNEH QSLGEGQTTT TTITYTITDP SGATSTATLT VTVTGTNDAP TLTPGVPLGD
QANDDGEAIA PVDISGQFQD IDKGDTLTFT ANGLPPGLTL DPATGIISGT LDNSASQGGN
NGVYTVTITA TDSGGKSVSQ TFEWDVTNPA PTAVADTGAT DEDTTLTVTD PAQGVLRNDT
DPDNDDLHVS AVNGQPANVG AAIAGDNGGT FTLNADGTYT FNPGPDFQNL AKDATAETSI
TYTVSDGEGG TSSATLTVTV TGTNDAPTLT PNVTLDDQAN NDGEAITPVD ISGQFEDVDN
GDTLTFTADG LPPGLTLDPA TGIISGTLDN SASQGGANND GVYTVEITAT DANGASVSQT
FEWDVNNPAP TAVAATGTTD EDTTLTVTDP AQGVLRNDTD PDNDDLHVSA VNGQPGNVGV
AIAGDNGGTF TLNADGTYSF NPGNAFQHLA QGDSVETSIS YTVSDGEGGT STTTLTVTVT
GVNDTGAISV NLGADDGKVY EAGLDNPADD SETTGGTITV SASDGISSVT IGGQTFTVAQ
LSGDLSSLPA INTTEGTLTI TGYTPSADGK SADITFSYTL NEAQTHSQPG NDTITDNIGV
TVTGNGDSET SSSFNITIVD DVPTFQTVTD TVLANEAGQT QTGTLEFESG ADGVGSLNIT
GITGLPNDWT TSAMNNASVN IFSPDGTHVF TVTLNTDGTY TVDQLATRPG TTESVNMGSQ
ITNSPQASYD FGIASVTVLH SNQQAQFNGK GSNVPNVSHE FGIGNTWFEG GESFQMTFES
PMLNFNFGIA TVNNPGSVKV TLFDGVNTLT LTVPVNAGDT SLSITQDQIQ AAAAAAVPPI
SFGEFSTATL EGVGGLKVSL TTLSYTNSVP ADDMDFTVHV TGTDGDGDPA QTEFDVTSGA
EAAVVDAFNR VMEDSGDTVG GSVMLSTALA VVSVSVNGTD VTNATAGNPV TFHTGKGTLV
VTGYDPQTGA LSYTYTEKGQ AHNHGNGKNS VHDDFTVTDS DGQERSGDLV IQILDSVPTA
HADLDNVTEG VTQNVSAADG VLANDTSADG WHHAGAIVGV AAGDTGAISH GKVGQAIDGL
YGKLTLNADG SYSYKANASG QGALPGDGQD VFTYTVRDAD GDLTSTTLTI NIDQFVAGSN
DNNTITGGAG NDVMLGDQGG IKQNVTAGTS YNIALVLDLS DSMNDKWGSG SNKPTRLQTA
KDALKALLEN QLAVHDGEIN VSLITFNGSS SALKKSITGL TPENVDEMVD ILMGLKASST
TPYGAAFDRT TQWFESQPTV DSEGKPYKNL TFFLTDGEPS TEWSYNRDNE FAELAAISDV
HGIGIGSGVS TSTLNKYDNT GGYYTGGQET HVNFSGNSNA NNVNTWDKDG TGTVTKNDNA
MRITDTTADG QAFKVTMNPD HRMNVTSAGG ASFSFALSMG NKNPADKFEW VLMKWDGTQW
NEVERGTDAS TRTGIHGPGQ YGFQFIVNDN SGGGQFYATV DTIRSYTSGR TGNSQTVLDP
SDLESALIGG SQSTELAPVG NDKLYGGDGN DILFGDAINT DNLPWGVAGN PAKPADLPNG
SGLEALKDFL FLKNGVQPTD ADLHKYISEN HALFDVDGDT RGGNDELHGG AGNDILYGQG
GNDKLYGGDG DDILYGGAGT DELRGGAGSD ELHGGEGKDL LIGGQGDDIL YGGDGSDTFK
WELNDQGVVG APARDTIKDF SNADIADGGD VLDLGELLQG ENSGNLTQFL KFSSDGQDTV
IQVNTQGHVN TQGADQTIVL ENIDLTAGGT KDDAAIIQDL LSRHKLQVDQ
//