FRPC_NEIMC
ID FRPC_NEIMC Reviewed; 1829 AA.
AC P55127;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Iron-regulated protein FrpC;
GN Name=frpC;
OS Neisseria meningitidis serogroup C.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=135720;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FAM20 / Serogroup C;
RX PubMed=8412674; DOI=10.1111/j.1365-2958.1993.tb01671.x;
RA Thompson S.A., Wang L.L., Sparling P.F.;
RT "Cloning and nucleotide sequence of frpC, a second gene from Neisseria
RT meningitidis encoding a protein similar to RTX cytotoxins.";
RL Mol. Microbiol. 9:85-96(1993).
CC -!- FUNCTION: May participate in the pathogenesis of meningococcal disease.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein.
CC Secreted.
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; L06299; AAA99902.1; -; Genomic_DNA.
DR PIR; S35027; S35027.
DR PDB; 6SJW; NMR; -; A=415-591.
DR PDB; 6SJX; NMR; -; A=416-591.
DR PDBsum; 6SJW; -.
DR PDBsum; 6SJX; -.
DR AlphaFoldDB; P55127; -.
DR BMRB; P55127; -.
DR SMR; P55127; -.
DR PRIDE; P55127; -.
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; -; 9.
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 InterPro; IPR028974; TSP_type-3_rpt.
DR Pfam; PF06594; HCBP_related; 4.
DR Pfam; PF00353; HemolysinCabind; 11.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF103647; SSF103647; 1.
DR SUPFAM; SSF51120; SSF51120; 6.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 17.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Membrane; Repeat; Secreted;
KW Toxin; Virulence.
FT CHAIN 1..1829
FT /note="Iron-regulated protein FrpC"
FT /id="PRO_0000196245"
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 STRAND 416..418
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:6SJW"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:6SJX"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:6SJW"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:6SJW"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:6SJX"
FT TURN 536..540
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 559..569
FT /evidence="ECO:0007829|PDB:6SJW"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:6SJW"
FT TURN 586..590
FT /evidence="ECO:0007829|PDB:6SJW"
SQ SEQUENCE 1829 AA; 197624 MW; 5C3494020A782DC8 CRC64;
MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DNAAAIVGKD TNLNGLNLWM
KKGVENLWDD TVGKKTRLEK FDRVALQHFS QYVDLINKNN GRLPNTSEIE RSYYKAVTYH
GVSSSAAIDL VINRSLPDMA DGYWALGLGI EAERIHNEQA VNNPNGSERD NRKQLISALD
KGFDGSFKEK HFTFLQSVMM DLTKLGVEYT IDGWQKIGGW GNGIINDLYK SVVKREWTGI
FEIVNNNIKQ GNEAFKNEIN SLVHDMKAAG KEFGDDLNTQ WNNLTQAAEI IYNDIVDNTS
QGIEKGVKAI KELSEKMKNA ASDLADGSAE KAKQVVEDLA QAAKEAYENA KSTAEKAAQA
AREFFKGLPS FKDLAEKFRD LFPNPEGWID DGHQCFAPWV KETKKRNGKY HVYDPLALDL
DGDGIETVAT KGFSGSLFDH NRDGIRTATG WVAADDGLLV 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
GQDSSTLYYM SEEDALNIVK VTNDTYDHLA KNIYQNLLFQ TRLQPYLNQI SFKMENDTFT
LDFSGLVQAF NHVKETNPQK AFVDLAEMLA YGELRSWYEG RRLMADYVEE AKKAGKFEDY
QKVLGQETVA LLAKTSGTQA DDILQNVGFG HNKNVSLYGN DGNDTLIGGA GNDYLEGGSG
SDTYVFGKGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDDSGQVT
VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD
DYLYGADGDD LLNGDAGNDS IYSGNGNDTL NGGEGNDALY GYNGNDALNG GEGNDHLNGE
DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT
FTREGNHLLI KAKDGSGQVT VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD
GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY
GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDTVYNYDY
ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDDSGQVT VQSYFQNDGS GAYRIDEIHF
DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GSTLNGGLGD DYLYGADGDD LLNGDAGNDS
IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG
SDTYVFGKGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT
VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKKLVQQSTD GSDRLYAYQS GNTLNGGLGD
DYLYGADGDD LLNGDAGNDS IYSGNGNDTL NGGEGNDALY GYNGNDVLNG GEGNDHLNGE
DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDTVYNYHV DKNSDTMHFK GFKAADVHFI
RSGSDLVLSA SEQDNVRISG FFYGENHRVD TFVFDDAAIS NPDFAKYINA GNNLVQSMSV
FGSNTAATGG NVDANTQSVQ QPLLVTPSA
