H8_NEIMA
ID H8_NEIMA Reviewed; 183 AA.
AC P57025; A1ISV0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Outer membrane protein H.8;
DE Flags: Precursor;
GN OrderedLocusNames=NMA1733;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; AL157959; CAM08862.1; -; Genomic_DNA.
DR PIR; E81797; E81797.
DR RefSeq; WP_002216827.1; NC_003116.1.
DR AlphaFoldDB; P57025; -.
DR SMR; P57025; -.
DR EnsemblBacteria; CAM08862; CAM08862; NMA1733.
DR KEGG; nma:NMA1733; -.
DR HOGENOM; CLU_112845_0_0_4; -.
DR OMA; MGHNFVL; -.
DR BioCyc; NMEN122587:NMA_RS08755-MON; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd13922; Azurin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR014068; Azurin.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR Pfam; PF00127; Copper-bind; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02695; azurin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Copper; Electron transport; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..183
FT /note="Outer membrane protein H.8"
FT /id="PRO_0000002854"
FT DOMAIN 57..183
FT /note="Plastocyanin-like"
FT REGION 27..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 183 AA; 18620 MW; FB355F6D02F2172D CRC64;
MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAAEAPASEA PAAEAAPADA AEAPAAGNCA
ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKTSM GHNIVIGKTE DMDGIFKDGV
GAADTDYVKP DDARVVAHTK LIGGGEESSL TLDPAKLADG EYKFACTFPG HGALMNGKVT
LVD