PFBA_STRR6
ID PFBA_STRR6 Reviewed; 719 AA.
AC Q8CYC9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Plasmin and fibronectin-binding protein A;
DE Flags: Precursor;
GN Name=pfbA; OrderedLocusNames=spr1652;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP SUBCELLULAR LOCATION, BINDING TO HOST EXTRACELLULAR MATRIX COMPONENTS,
RP PROBABLE INVOLVEMENT IN VIRULENCE, BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RX PubMed=18974092; DOI=10.1074/jbc.m807087200;
RA Yamaguchi M., Terao Y., Mori Y., Hamada S., Kawabata S.;
RT "PfbA, a novel plasmin- and fibronectin-binding protein of Streptococcus
RT pneumoniae, contributes to fibronectin-dependent adhesion and
RT antiphagocytosis.";
RL J. Biol. Chem. 283:36272-36279(2008).
CC -!- FUNCTION: Acts as a fibronectin-dependent adhesin and invasin. Binds
CC host (in this case human) fibronectin, plasmin, plasminogen, and human
CC serum albumin. Where the bacteria adhere to human cells there is major
CC recruitment of microvilli which seem to fuse to cover the streptococcal
CC chains. Antibodies to this protein reduce bacterial growth in human
CC blood.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:18974092}; Peptidoglycan-anchor
CC {ECO:0000305|PubMed:18974092}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene adhere to and invade
CC human cell lines half as well as wild-type bacteria. They grow less
CC well in human blood, perhaps because they are more resistant to
CC phagocytosis. {ECO:0000269|PubMed:18974092}.
CC -!- BIOTECHNOLOGY: Has potential use as a vaccine component.
CC {ECO:0000269|PubMed:18974092}.
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DR EMBL; AE007317; AAL00455.1; -; Genomic_DNA.
DR PIR; B98078; B98078.
DR RefSeq; NP_359244.1; NC_003098.1.
DR RefSeq; WP_010976622.1; NC_003098.1.
DR PDB; 4MR0; X-ray; 1.95 A; A/B=150-607.
DR PDBsum; 4MR0; -.
DR AlphaFoldDB; Q8CYC9; -.
DR SMR; Q8CYC9; -.
DR STRING; 171101.spr1652; -.
DR EnsemblBacteria; AAL00455; AAL00455; spr1652.
DR GeneID; 60234187; -.
DR KEGG; spr:spr1652; -.
DR PATRIC; fig|171101.6.peg.1781; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_389752_0_0_9; -.
DR OMA; VLMKYFV; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Coiled coil; Peptidoglycan-anchor;
KW Reference proteome; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..688
FT /note="Plasmin and fibronectin-binding protein A"
FT /id="PRO_0000380122"
FT PROPEP 689..719
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000380123"
FT REPEAT 287..310
FT /note="PbH1 1"
FT REPEAT 362..384
FT /note="PbH1 2"
FT REPEAT 397..419
FT /note="PbH1 3"
FT REPEAT 497..523
FT /note="PbH1 4"
FT REPEAT 525..546
FT /note="PbH1 5"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 601..658
FT /evidence="ECO:0000255"
FT MOTIF 685..689
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 619..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 688
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4MR0"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:4MR0"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 279..294
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:4MR0"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:4MR0"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:4MR0"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:4MR0"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:4MR0"
SQ SEQUENCE 719 AA; 79016 MW; 5A4E3047262CBFBD CRC64;
MLKIVKKLEV LMKYFVPNEV FSIRKLKVGT CSVLLAISIL GSQGILSDEV VTSSSPMATK
ESSNAITNDL DNSPTVNQNR SAEMIASNST TNGLDNSLSV NSISSNGTIR SNSQLDNRTV
ESTVTSTNEN KSYKEDVISD RIIKKEFEDT ALSVKDYGAV GDGIHDDRQA IQDAIDAAAQ
GLGGGNVYFP EGTYLVKEIV FLKSHTHLEL NEKATILNGI NIKNHPSIVF MTGLFTDDGA
QVEWGPTEDI SYSGGTIDMN GALNEEGTKA KNLPLINSSG AFAIGNSNNV TIKNVTFKDS
YQGHAIQIAG SKNVLVDNSR FLGQALPKTM KDGQIISKES IQIEPLTRKG FPYALNDDGK
KSENVTIQNS YFGKSDKSGE LVTAIGTHYQ TLSTQNPSNI KILNNHFDNM MYAGVRFTGF
TDVLIKGNRF DKKVKGESVH YRESGAALVN AYSYKNTKDL LDLNKQVVIA ENIFNIADPK
TKAIRVAKDS AEYLGKVSDI TVTKNVINNN SKETEQPNIE LLRVSDNLVV SENSIFGGKE
GIVIEDSKGK ITVLNNQFYN LSGKYISFIK SNANGKEPVI RDSDGNFNIV TENGLYKIVT
NNLSDKNEKE KNKEEKQSNS NNVIDSNQKN GEFNSSKDNR QMNDKIDNKQ DNKTEEVNYK
IVGDGRETEN HINKSKEIVD VKQKLPKTGS NKIMELFLTV TGIGLLLTLK GLKYYGKDK
