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Database: UniProt
Entry: K0MBS3_BORPB
LinkDB: K0MBS3_BORPB
Original site: K0MBS3_BORPB 
ID   K0MBS3_BORPB            Unreviewed;       699 AA.
AC   K0MBS3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Type III secretion pore protein {ECO:0000313|EMBL:CCJ48707.1};
GN   Name=bcrD {ECO:0000313|EMBL:CCJ48707.1};
GN   OrderedLocusNames=BN117_1374 {ECO:0000313|EMBL:CCJ48707.1};
OS   Bordetella parapertussis (strain Bpp5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ48707.1, ECO:0000313|Proteomes:UP000008035};
RN   [1] {ECO:0000313|EMBL:CCJ48707.1, ECO:0000313|Proteomes:UP000008035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ48707.1,
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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export
CC       pore) family. {ECO:0000256|ARBA:ARBA00008835}.
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DR   EMBL; HE965803; CCJ48707.1; -; Genomic_DNA.
DR   RefSeq; WP_015039314.1; NC_018828.1.
DR   RefSeq; YP_006895356.1; NC_018828.1.
DR   AlphaFoldDB; K0MBS3; -.
DR   KEGG; bpar:BN117_1374; -.
DR   HOGENOM; CLU_015346_3_0_4; -.
DR   Proteomes; UP000008035; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 3.40.30.60; FHIPEP family, domain 1; 1.
DR   Gene3D; 1.10.8.540; FHIPEP family, domain 3; 1.
DR   Gene3D; 3.40.50.12790; FHIPEP family, domain 4; 1.
DR   InterPro; IPR042194; FHIPEP_1.
DR   InterPro; IPR042193; FHIPEP_3.
DR   InterPro; IPR042196; FHIPEP_4.
DR   InterPro; IPR025505; FHIPEP_CS.
DR   InterPro; IPR001712; T3SS_FHIPEP.
DR   InterPro; IPR006302; T3SS_HrcV.
DR   NCBIfam; TIGR01399; hrcV; 1.
DR   PANTHER; PTHR30161; FLAGELLAR EXPORT PROTEIN, MEMBRANE FLHA SUBUNIT-RELATED; 1.
DR   PANTHER; PTHR30161:SF2; INVASION PROTEIN INVA; 1.
DR   Pfam; PF00771; FHIPEP; 1.
DR   PIRSF; PIRSF005419; FlhA; 1.
DR   PRINTS; PR00949; TYPE3IMAPROT.
DR   PROSITE; PS00994; FHIPEP; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   699 AA;  75457 MW;  357EE95FC3362B84 CRC64;
     MTSKKSILRL QRAVALATSR NDIVLAVLIV AIVFMMILPL PTTLVDVLIG ANMTLSAVLL
     MVAMYLPSPL AFSSFPSVLL VTTLFRLGIS IATTRLILLQ GDAGHIIETF GNFVVGGNLI
     VGLVVFLILT IVQFVVITKG AERVAEVAAR FSLDAMPGKQ MSIDADLRAG TIDMDEARRR
     RRTVEKESQL YGAMDGAMKF VKGDAIAGLI IVAVNLLGGM LVGVLQRGLS AGEAVQTYAI
     LTIGDGLIAQ IPALFIAICA GIIVTRVQTG DGPSNVGTDI GAQVLAQPRA LVIAGAISAG
     LGLIPGMPTL VFFALAAVVG TIGFVLLRAS QRPPEGAGPA LAGMAADGQP RTRAPADGQA
     EFAPTVPLII DVAARLQPRF EPATLTDDLL QIRRALYFDL GVPFPGIQLR FTEALAANTY
     TIVLSEIPVA QGMLRDDAVL VRDTEQNLQA LRIAYETGAA FLPDTPTIWV TASLTGALRD
     AGIPYLGISQ ILTWHLAYVL KKYSADFIGI QETRFLLSAM EERFPDLVKE CLRVMPVQKI
     AEILQRLVSE EVSIRNLRAV LEALVEWGQK EKDTVLLTEY VRIALKRYIS YKYTSGHNIL
     PAYLLAPKVE ETVRAAIRQT AAGSYLALDP DTTRRLVEHI RQCVGDLAAG ASRPVLLTSM
     DIRRYTRKMI EADLYALPVL SYQELTPEIN VQPLGRVDL
//
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