ID   FRPC_NEIMB              Reviewed;        1829 AA.
AC   Q9JYV5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Iron-regulated protein FrpC;
GN   Name=frpC; OrderedLocusNames=NMB1415;
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; AAF41776.1; -; Genomic_DNA.
DR   PIR; E81086; E81086.
DR   RefSeq; NP_274427.1; NC_003112.2.
DR   RefSeq; WP_010980934.1; NC_003112.2.
DR   AlphaFoldDB; Q9JYV5; -.
DR   SASBDB; Q9JYV5; -.
DR   SMR; Q9JYV5; -.
DR   STRING; 122586.NMB1415; -.
DR   PaxDb; Q9JYV5; -.
DR   EnsemblBacteria; AAF41776; AAF41776; NMB1415.
DR   KEGG; nme:NMB1415; -.
DR   PATRIC; fig|122586.8.peg.1767; -.
DR   HOGENOM; CLU_001954_0_1_4; -.
DR   OMA; HEYYQFE; -.
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; -; 7.
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; 4.
DR   Pfam; PF00353; HemolysinCabind; 10.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SUPFAM; SSF51120; SSF51120; 5.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 17.
PE   3: Inferred from homology;
KW   Calcium; Cell outer membrane; Membrane; Reference proteome; Repeat;
KW   Secreted; Toxin; Virulence.
FT   CHAIN           1..1829
FT                   /note="Iron-regulated protein FrpC"
FT                   /id="PRO_0000196244"
FT   REPEAT          869..886
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          887..904
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REPEAT          1015..1032
FT                   /note="Hemolysin-type calcium-binding 3"
FT   REPEAT          1033..1050
FT                   /note="Hemolysin-type calcium-binding 4"
FT   REPEAT          1051..1068
FT                   /note="Hemolysin-type calcium-binding 5"
FT   REPEAT          1069..1086
FT                   /note="Hemolysin-type calcium-binding 6"
FT   REPEAT          1087..1104
FT                   /note="Hemolysin-type calcium-binding 7"
FT   REPEAT          1215..1232
FT                   /note="Hemolysin-type calcium-binding 8"
FT   REPEAT          1233..1250
FT                   /note="Hemolysin-type calcium-binding 9"
FT   REPEAT          1251..1268
FT                   /note="Hemolysin-type calcium-binding 10"
FT   REPEAT          1269..1286
FT                   /note="Hemolysin-type calcium-binding 11"
FT   REPEAT          1287..1304
FT                   /note="Hemolysin-type calcium-binding 12"
FT   REPEAT          1415..1432
FT                   /note="Hemolysin-type calcium-binding 13"
FT   REPEAT          1433..1450
FT                   /note="Hemolysin-type calcium-binding 14"
FT   REPEAT          1451..1468
FT                   /note="Hemolysin-type calcium-binding 15"
FT   REPEAT          1469..1486
FT                   /note="Hemolysin-type calcium-binding 16"
FT   REPEAT          1487..1504
FT                   /note="Hemolysin-type calcium-binding 17"
FT   REPEAT          1615..1632
FT                   /note="Hemolysin-type calcium-binding 18"
FT   REPEAT          1633..1650
FT                   /note="Hemolysin-type calcium-binding 19"
FT   REPEAT          1651..1668
FT                   /note="Hemolysin-type calcium-binding 20"
FT   REPEAT          1669..1686
FT                   /note="Hemolysin-type calcium-binding 21"
FT   REPEAT          1687..1704
FT                   /note="Hemolysin-type calcium-binding 22"
FT   REGION          1671..1690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1829 AA;  197446 MW;  8F63506E1F6D9B40 CRC64;
     MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DDAAAIVGKD ANLNGLNLWM
     KKGVENLWDD TVGKKTRLEK FDRVALQHFR QYARLINQNN GRLPNTSEIE RSYYKAVTDN
     GVSSSAAIDL VINRSLPDMA DGYWALGLGI EAERIHNEQA VNNPNGSERD NRKQLISALD
     KGFDGSFKEK HFTFLQSVMM DVTKLGVEYT IDGWQKIGGW GNGIINDLYK SVVKREWTGI
     FEIVNNNIKQ GNEAFKNEIN SLVHDMKAAG KEFGDDLNTQ WNNLTQAAEI IYNDIVDNTS
     QGIEKGVKAI KELSEKMKNA ASDLADGSAE KAKQVVEDLA QAAKEAYENA KSTAEKAAQA
     AREFFKGLPS FKDLAEKFRD LFPNPEGWID DGHQCLAPWV KETKKRNGKY HVYDPLALDL
     DGDGIETVAT KGFAGSLFDH TNNGIRTATG WVSADDGLLV RDLNGNGIID NGAELFGDNT
     KLADGSFAKH GYAALAELDS NGDNIINAAD AAFQTLRVWQ DLNQDGISQA NELRTLEELG
     IQSLDLAYKD VNKNLGNGNT LAQQGSYTKT DGTTAKMGDL LLAADNLHSR FKDKVELTAE
     QAKAANLAGI GRLRDLREAA ALSGDLANML KAYSAAETKE AQLALLDNLI HKWAETDSNW
     GKKSPMRLST DWTQTANEGI ALTPSQVAQL KKNALVSLSD KAKAAIDAAR DRIAVLDAYT
     GQDSNTLYYM SEEDALNIVK VTNDTYDHLA KNIYQNLLFQ TRLQPYLNQI SFKMENDTFT
     LDFSGLVQAF NHVKETNPQK AFVDLAEMLA YGELRSWYEG RRLMTDYVEE AKKAGKFEDY
     QKVLGQETVA LLAKTSGTQA DDILQNVGFG HNKNVSLYGN DGNDTLIGGA GNDYLEGGSG
     SDTYVFGEGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT
     VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD
     DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE
     DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT
     FTREGNHLLI KAKDGSGQVT VQYYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD
     GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY
     GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDAVYNYDY
     ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT VQSYFQNDGS GAYRIDEIHF
     DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS
     IYSGNGNDTL NGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG
     SDTYVFGKGF GQDAVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT
     VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GSTLNGGLGD
     DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE
     DGNDTLIGGA GNDYLEGGSG SDTYVFGEGF GQDTVYNYHV DKNSDTMHFK GFKAADVHFI
     RSGSDLVLSA SEQDNVRISG FFYGENHRVD TFVFDDAAIS NPDFAKYINA GNNLVQSMSV
     FGSNTAATGG NVDANIQSVQ QPLLVTPSA