ID E3D458_NEIM7 Unreviewed; 152 AA.
AC E3D458;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=C-type cytochrome {ECO:0000313|EMBL:ADO31415.1};
GN OrderedLocusNames=NMBB_1036 {ECO:0000313|EMBL:ADO31415.1};
OS Neisseria meningitidis serogroup B (strain alpha710).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO31415.1, ECO:0000313|Proteomes:UP000006929};
RN [1] {ECO:0000313|EMBL:ADO31415.1, ECO:0000313|Proteomes:UP000006929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX PubMed=20709895; DOI=10.1128/JB.00883-10;
RA Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT "Comparative genome biology of a serogroup B carriage and disease strain
RT supports a polygenic nature of meningococcal virulence.";
RL J. Bacteriol. 192:5363-5377(2010).
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
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DR EMBL; CP001561; ADO31415.1; -; Genomic_DNA.
DR RefSeq; WP_002223449.1; NC_017505.1.
DR AlphaFoldDB; E3D458; -.
DR KEGG; nmp:NMBB_1036; -.
DR PATRIC; fig|630588.3.peg.1204; -.
DR HOGENOM; CLU_106713_4_0_4; -.
DR Proteomes; UP000006929; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.20.120.10; Cytochrome c/b562; 1.
DR InterPro; IPR010980; Cyt_c/b562.
DR InterPro; IPR002321; Cyt_c_II.
DR InterPro; IPR012127; Cyt_c_prime.
DR InterPro; IPR015984; Cyt_c_prime_subgr.
DR Pfam; PF01322; Cytochrom_C_2; 1.
DR PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR PRINTS; PR00608; CYTCHROMECII.
DR SUPFAM; SSF47175; Cytochromes; 1.
DR PROSITE; PS51009; CYTCII; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000027-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000027-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000027-1}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..152
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003168259"
FT BINDING 141
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT BINDING 144
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT BINDING 145
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-1"
SQ SEQUENCE 152 AA; 16193 MW; EB2E9C2A2D4E3CCA CRC64;
MNIQTRLAAT ALALFLSACG NGGAPAQPKG EISENRTAAF KSMMPDFSRM GKMVKGEEPY
DVEKFKQATA SFAESSKKPF TLFESDPQGN GRALPAVWSD GAKFEAEKTK FAAAVEKLNA
AAQTGKLDEI KAAYGETGAS CKSCHDSFRA PE
//
