FRPA_NEIMB
ID FRPA_NEIMB Reviewed; 1302 AA.
AC Q9K0K9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Iron-regulated protein FrpA;
GN Name=frpA; OrderedLocusNames=NMB0585;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: May participate in the pathogenesis of meningococcal disease.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Secreted {ECO:0000250}.
CC -!- DOMAIN: The Gly-rich region is probably involved in binding calcium,
CC which is required for target cell-binding or cytolytic activity.
CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF41013.1; -; Genomic_DNA.
DR PIR; C81182; C81182.
DR RefSeq; NP_273629.1; NC_003112.2.
DR RefSeq; WP_010980816.1; NC_003112.2.
DR AlphaFoldDB; Q9K0K9; -.
DR SMR; Q9K0K9; -.
DR STRING; 122586.NMB0585; -.
DR PaxDb; Q9K0K9; -.
DR EnsemblBacteria; AAF41013; AAF41013; NMB0585.
DR KEGG; nme:NMB0585; -.
DR PATRIC; fig|122586.8.peg.747; -.
DR HOGENOM; CLU_001954_0_1_4; -.
DR OMA; YFYSAEY; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 5.
DR InterPro; IPR010566; Haemolys_ca-bd.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF06594; HCBP_related; 2.
DR Pfam; PF00353; HemolysinCabind; 5.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; SSF51120; 3.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 9.
PE 3: Inferred from homology;
KW Calcium; Cell outer membrane; Membrane; Reference proteome; Repeat;
KW Secreted; Toxin; Virulence.
FT CHAIN 1..1302
FT /note="Iron-regulated protein FrpA"
FT /id="PRO_0000196242"
FT REPEAT 742..759
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 760..777
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 888..905
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 906..923
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 924..941
FT /note="Hemolysin-type calcium-binding 5"
FT REPEAT 942..959
FT /note="Hemolysin-type calcium-binding 6"
FT REPEAT 960..977
FT /note="Hemolysin-type calcium-binding 7"
FT REPEAT 1088..1105
FT /note="Hemolysin-type calcium-binding 8"
FT REPEAT 1106..1123
FT /note="Hemolysin-type calcium-binding 9"
FT REPEAT 1124..1141
FT /note="Hemolysin-type calcium-binding 10"
FT REPEAT 1142..1159
FT /note="Hemolysin-type calcium-binding 11"
FT REPEAT 1160..1177
FT /note="Hemolysin-type calcium-binding 12"
FT REGION 1144..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 141398 MW; 21D058C56C98BDE8 CRC64;
MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DDAAAIVGKD ANLNGLNLWM
KKGVENLWDD TVGKKTRLEK FDRVALQHFS QYVDLINENN GRLPNTSEIE RSYYKAVTEN
GVSSSAAIDL VINRSLPDMA DGYWALGLGI EAERIHNEQA VNNPNGSERD NRKQLISALD
KGFDGSFKEK HFTFLQSVIM DVTKLGVEYT IDGWQKIGGW GNGIINDLYK SVVKREWTGI
FEIVNNNIKQ FRDLFPNPEG WIDDGHQCFA PWVKETKKRN GKYHVYDPLA LDLDGDGIET
VAAKGFSGSL FDHTNNGIRT ATGWVSADDG LLVRDLNGNG IIDNGAELFG DNTKLADGSF
AKHGYAALAE LDSNGDNIIN AADAAFQSLR VWQDLNQDGI SQANELRTLE ELGIQSLDLA
YKDVNKNLGN GNTLAQQGSY TKTDGTTAKM GDLLLAADNL HSRFKDKVEL TAEQAKAANL
AGIGRLRDLR EAAALSGDLA NMLKAYSAAE TKEAQLALLD NLIHKWAETD SNWGKKSPMR
LSTDWTQTAN EGIALTPSQV AQLKKNALVS LSDKAKAAID AARDRIAVLD AYTGQDSNTL
YYMSEEDALN IVKVTNDTYD HLAKNIYQNL LFQTRLQPYL NQISFKMEND TFTLDFSGLV
QAFNHVKETN PQKAFVDLAE MLAYGELRSW YEGRRLMTDY VEEAKKAGKF EDYQKVLGQE
TVALLAKTSG TQADDILQNV GFGHNKNVSL YGNDGNDTLI GGAGNDYLEG GSGSDTYVFG
EGFGQDTVYN YDYATGRKDI IRFTDGITAD MLTFTREGNH LLIKAKDGSG QVTVQSYFQN
DGSGAYRIDE IHFDNGKVLD VATVKELVQQ STDGSDRLYA YQSGNTLNGG LGDDYLYGAD
GDDLLNGDAG NDSIYSGNGN DTLDGGEGND ALYGYNGNDA LNGGEGNDHL NGEDGNDTLI
GGAGNDYLEG GSGSDTYVFG KGFGQDAVYN YDYATGRKDI IRFTDGITAD MLTFTREGNH
LLIKAKDGSG QVTVQSYFQN DGSGAYRIDE IHFDNGKVLD VATVKELVQQ STDGSDRLYA
YQSGNTLNGG LGDDYLYGAD GDDLLNGDAG NDSIYSGNGN DTLDGGEGND ALYGYNGNDA
LNGGEGNDHL NGEDGNDTLI GGAGNDYLEG GSGSDTYVFG EGFGQDTVYN YHVDKNSDTM
HFKGFKAADV HFIRSGSDLV LSASEQDNVR ISGFFYGENH RVDTFVFDDA AISNPDFAKY
INAGNNLVQS MSVFGSNTAA TGGNVDANIQ SVQQPLLVTP SA
