ID   H81_NEIGO               Reviewed;         183 AA.
AC   P07211;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Outer membrane protein H.8;
DE   Flags: Precursor;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DIACYLGLYCEROL AT CYS-18.
RC   STRAIN=R10;
RA   Godschlich E.C., Seiff M.E.;
RT   "Identification and gene structure of an azurin-like protein with a
RT   lipoprotein signal peptide in Neisseria gonorrhoeae.";
RL   FEMS Microbiol. Lett. 43:253-255(1987).
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; Lipid-anchor.
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DR   EMBL; X06208; CAA29561.1; -; Genomic_DNA.
DR   PIR; S06374; AZNHG.
DR   RefSeq; WP_003688275.1; NZ_WHPL01000002.1.
DR   AlphaFoldDB; P07211; -.
DR   BMRB; P07211; -.
DR   SMR; P07211; -.
DR   GeneID; 66753316; -.
DR   OMA; MGHNFVL; -.
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   1: Evidence at protein level;
KW   Cell outer membrane; Copper; Electron transport; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Signal; Transport.
FT   SIGNAL          1..17
FT   CHAIN           18..183
FT                   /note="Outer membrane protein H.8"
FT                   /id="PRO_0000002853"
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:0000305"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|Ref.1"
SQ   SEQUENCE   183 AA;  18532 MW;  50EEAB89163277EC CRC64;
     MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAGEAPASEA PAAEAAPADA AEAPAAGNCA
     ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKASM GHNLVIAKAE DMDGVFKDGV
     GAADTDYVKP DDARVVAHTK LIGGGEESSL TLDPAKLADG DYKFACTFPG HGALMNGKVT
     LVD