ID Q7DD79_NEIMB Unreviewed; 207 AA.
AC Q7DD79;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Cytochrome c4 {ECO:0000313|EMBL:AAF42142.1};
GN OrderedLocusNames=NMB1805 {ECO:0000313|EMBL:AAF42142.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42142.1, ECO:0000313|Proteomes:UP000000425};
RN [1] {ECO:0000313|EMBL:AAF42142.1, ECO:0000313|Proteomes:UP000000425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42142.1,
RC ECO:0000313|Proteomes:UP000000425};
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J., 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., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H., Qin H., Vamathevan 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000005-1}.
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DR EMBL; AE002098; AAF42142.1; -; Genomic_DNA.
DR PIR; F81040; F81040.
DR RefSeq; NP_274802.1; NC_003112.2.
DR RefSeq; WP_002214509.1; NC_003112.2.
DR AlphaFoldDB; Q7DD79; -.
DR STRING; 122586.NMB1805; -.
DR PaxDb; 122586-NMB1805; -.
DR GeneID; 61280702; -.
DR KEGG; nme:NMB1805; -.
DR PATRIC; fig|122586.8.peg.2295; -.
DR HOGENOM; CLU_076280_2_1_4; -.
DR InParanoid; Q7DD79; -.
DR OrthoDB; 9773456at2; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR024167; Cytochrome_c4-like.
DR PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR PANTHER; PTHR33751:SF9; CYTOCHROME C4; 1.
DR Pfam; PF00034; Cytochrom_C; 2.
DR PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000005-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000005-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000005-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000425};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..207
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004287259"
FT DOMAIN 22..207
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT BINDING 39
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT BINDING 81
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT BINDING 135
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT BINDING 138
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT BINDING 139
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT BINDING 184
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
SQ SEQUENCE 207 AA; 21989 MW; 29C843B52987AA0D CRC64;
MKRLTLLAFV LAAGAVSASP KADVEKGKQV AATVCAACHA ADGNSGIAMY PRLAAQHTAY
IYHQTIGIRD GKRTHGSAAV MKPVVMNLSD QDILNVSAFY AKQQPKSGEA NPKENPELGA
KIYRGGLSDK KVPACMSCHG PSGAGMPGGG SEIQAYPRLG GQHQAYIVEQ MNAYKSGQRK
NTIMEDIANR MSEEDLKAVA NFIQGLR
//
