FHAC_BORPE
ID FHAC_BORPE Reviewed; 584 AA.
AC P35077;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Filamentous hemagglutinin transporter protein FhaC;
DE AltName: Full=TpsB transporter;
DE Flags: Precursor;
GN Name=fhaC; OrderedLocusNames=BP1884;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wellcome 28;
RA Willems R.J.L.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Tohama I / BPSM;
RX PubMed=16771844; DOI=10.1111/j.1365-2958.2006.05242.x;
RA Hodak H., Clantin B., Willery E., Villeret V., Locht C.,
RA Jacob-Dubuisson F.;
RT "Secretion signal of the filamentous haemagglutinin, a model two-partner
RT secretion substrate.";
RL Mol. Microbiol. 61:368-382(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-584, FUNCTION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS.
RC STRAIN=Tohama I / BPSM;
RX PubMed=17702945; DOI=10.1126/science.1143860;
RA Clantin B., Delattre A.S., Rucktooa P., Saint N., Meli A.C., Locht C.,
RA Jacob-Dubuisson F., Villeret V.;
RT "Structure of the membrane protein FhaC: a member of the Omp85-TpsB
RT transporter superfamily.";
RL Science 317:957-961(2007).
CC -!- FUNCTION: Member of a two partner secretion pathway (TPS) in which it
CC mediates the secretion of filamentous hemagglutinin FHA (fhaB).
CC {ECO:0000269|PubMed:16771844, ECO:0000269|PubMed:17702945}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17702945}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16771844}.
CC -!- DOMAIN: In the crystal structure alpha helix H1 passes through the
CC middle of the pore with its C-terminus in the periplasm and loop L6
CC also blocks the channel. Both of the POTRA domains are periplasmic;
CC POTRA stands for polypeptide-transport associated.
CC {ECO:0000305|PubMed:17702945}.
CC -!- SIMILARITY: Belongs to the TPS (TC 1.B.20) family. {ECO:0000305}.
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DR EMBL; X64876; CAA46092.1; -; Genomic_DNA.
DR EMBL; BX640416; CAE42167.1; -; Genomic_DNA.
DR PIR; S41526; S41526.
DR RefSeq; NP_880575.1; NC_002929.2.
DR RefSeq; WP_010930614.1; NZ_CP039022.1.
DR PDB; 3NJT; X-ray; 3.50 A; A=34-584.
DR PDB; 4QKY; X-ray; 2.90 A; A=31-584.
DR PDB; 4QL0; X-ray; 2.50 A; A=31-584.
DR PDBsum; 3NJT; -.
DR PDBsum; 4QKY; -.
DR PDBsum; 4QL0; -.
DR AlphaFoldDB; P35077; -.
DR SMR; P35077; -.
DR IntAct; P35077; 1.
DR MINT; P35077; -.
DR STRING; 257313.BP1884; -.
DR TCDB; 1.B.20.1.6; the two-partner secretion (tps) family.
DR GeneID; 45389209; -.
DR KEGG; bpe:BP1884; -.
DR PATRIC; fig|257313.5.peg.2022; -.
DR eggNOG; COG2831; Bacteria.
DR HOGENOM; CLU_020581_4_1_4; -.
DR OMA; LGQFQWV; -.
DR EvolutionaryTrace; P35077; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005565; Hemolysn_activator_HlyB_C.
DR InterPro; IPR013686; Polypept-transport_assoc_ShlB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR035251; ShlB_POTRA.
DR InterPro; IPR027282; TPS.
DR Pfam; PF08479; POTRA_2; 1.
DR Pfam; PF17287; POTRA_3; 1.
DR Pfam; PF03865; ShlB; 1.
DR PIRSF; PIRSF029745; FhaC; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..584
FT /note="Filamentous hemagglutinin transporter protein FhaC"
FT /id="PRO_0000018666"
FT TRANSMEM 242..248
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 261..269
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 277..285
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 294..306
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 309..321
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 334..349
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 354..370
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 378..395
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 399..409
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 431..444
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 449..460
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 500..510
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 516..527
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 537..547
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 552..562
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT TRANSMEM 575..584
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:17702945"
FT DOMAIN 89..164
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 38..58
FT /note="Alpha helix H1, not required for FHA secretion"
FT /evidence="ECO:0000269|PubMed:17702945"
FT REGION 57..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..164
FT /note="POTRA 1; required for FHA secretion but not channel
FT formation"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17702945"
FT REGION 165..238
FT /note="POTRA 2; required for FHA secretion but not channel
FT formation"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17702945"
FT REGION 462..504
FT /note="Loop L6, required for FHA secretion and possibly for
FT channel stability"
FT /evidence="ECO:0000269|PubMed:17702945"
FT HELIX 36..61
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 257..269
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:4QL0"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 294..306
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 309..323
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 332..350
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 352..375
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 377..396
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 431..447
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 449..460
FT /evidence="ECO:0007829|PDB:4QL0"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:4QL0"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 488..501
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 513..527
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:3NJT"
FT STRAND 535..549
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 552..561
FT /evidence="ECO:0007829|PDB:4QL0"
FT STRAND 575..584
FT /evidence="ECO:0007829|PDB:4QL0"
SQ SEQUENCE 584 AA; 64446 MW; 8E625B2C07702178 CRC64;
MTDATNRFRP GLVGRALVRA GLLFAVAACA QAQLLPGARD LNRIDDRQRK EQLQRDIERA
LTRPPVELNP QSEAAAPARK PDATSGHTVT VHAVDLDFGV EGRLFDPAPL VQDYLNRPLD
NEQLFLLVKA LSAALYDRGY ATSIVTFVPP GVVDGVLKLK VEWGRIKGWL IDGKPLEGTR
DRMMVFSAMP GWQDKVLNVF DIDQAIYNIN NGGKTGNITI VPADEYGYSY LDLQLQRRAL
PRVSLGMDNS GPGTPENGRY KYNASVTAND LLGLNDTLGL YIGNRYYRDA GHDAERNYDL
MYSVPLGRTR LDLQTGYSTY RNLLKTRYGQ YQSAGNSRSF GLKATRLLYR DTRSQFSVYG
GLKLRQNKNY LAGTRLDVSS KHYSDVTVGM QYSTQRGANA YFGDLSFTRG VGVNNGKYAA
YDERGPQGNV SRFNGSLAWT RYMALAGQPI QWASQLGFQY SRQQLLNSYQ ITVGDEYTVR
GYNLRTSQSG DSGVYLSNTL TVPVQFSLLG KQASVAPFVG ADVGALKSNH PDARTIRMAG
LAAGVRFDLP YARMSFTYSK PVGAQPGGAP RAPVWLYINA GLSF
