ID Q39TN2_GEOMG Unreviewed; 1201 AA.
AC Q39TN2;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Laccase family multicopper oxidase {ECO:0000313|EMBL:ABB32392.1};
GN Name=ompB {ECO:0000313|EMBL:ABB32392.1};
GN OrderedLocusNames=Gmet_2163 {ECO:0000313|EMBL:ABB32392.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB32392.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB32392.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB32392.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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DR EMBL; CP000148; ABB32392.1; -; Genomic_DNA.
DR RefSeq; WP_011365924.1; NC_007517.1.
DR AlphaFoldDB; Q39TN2; -.
DR STRING; 269799.Gmet_2163; -.
DR KEGG; gme:Gmet_2163; -.
DR eggNOG; COG2132; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_001857_0_0_7; -.
DR Proteomes; UP000007073; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR Gene3D; 2.40.128.340; -; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR028994; Integrin_alpha_N.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF13517; FG-GAP_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1201
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004223382"
FT DOMAIN 779..852
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 1201 AA; 129400 MW; 028CF34CC0329D69 CRC64;
MNRQQLSIIM SLVLALAALP LAAYAGPGTR ATPPAPDYPA SATPSGGTFY ANSPAGPWKY
TNIMGTYSSA SSNSGTPLRK FVDSLPGLGS GARPAGTALG ANNLGQYIPI AAPDTATYPG
SDYYQIGLKD YRVQMHSDLP PTADALGTGT KLRGYYQKNG TDHSSNYLGP LIIAQKDRPV
RIKFFNELGA NGAGDLFIPV DTTYMGAGMG PNGMDNYTQN RADLHLHGGH SPWISDGTPH
QWITPAGETS TPYTSGASLR NVPDMDGGIE PAGASTYFWT NNQSGRMLFY HDHSYGITRL
NVYAGEAAGY LIVDPAEETS LAAAGVPGTI RNPANLGDTA NNDLAHIIPL IIQDKTFVPQ
DIAVQDTKWN DPKWGKYGDL WFPHVYETNQ WPTNPDLSGA NNFGRWDYGP WFWPIFPAAV
PGLPTMNVSG VPEGFMDTPV VNGTAYPYMD VQPQAYRLRI LNAANDRMFN LSFFTADPTL
TPFDPVTGQP NPGYQKEVKM VPAVPRPVCS ATVTTNCTCA GAPGTPVGCF PPTWPTDSRA
GGVPDPATAG PPIIQIGSEG GLLPAPTVIN PQPVNYEYNR RNVVVLNVSD KALFLGPAER
ADVIVDFSAY AGKTVILYND GPAPVPAFDP RNDYYTGCPD NTSSGGAPPT MAGYGPNTRT
IMQFRVAAAT PVPFNPAPLT TALPTIYAAS QPAPVIPQTG YPGPYKATAD TYSRISDNSL
TFTPVGATAP VTMPMKSKAI QELFTADYGR MNATLGVELP FTNALIQTTI PLGYIDPTTE
QLNNGQPQLW KITHNGVDTH AIHFHLFDVQ IINRVGWDGM IRPPDANELG WKDTVRMHPL
EDIVVAMRPT TPPVPFPLPN SVRPLDVTMP LGTTTQFTGV DPTTNTPITV TNELTNFEHE
YVWHCHLLGH EENDMMRPVV FATKPPQGDF NGLGKTDIAV WRPGTTGQWW IKTSTNTPVV
INQGITGDKL VPGDYDGDRK TDVAVWRPSD GNWYITNSAN GTTSTIGYGT NGDIPVPGDY
DGIGKTETAV WRPSNGTWYI PNSANGTQSV ITYGTNGDIP VAGDYDGDGK TDVAVWRPSN
GRWYIKNSGS TTQTVVSYGS NGDTPVPGDY DGDNKTDMAV WRNGTWYIKN SATNTQTVVN
FGTAGDIPVP GDYENLGRTE IAVWRPSNGN WYIMNPVTHL QTTVNWGAPT DLPIKVFQPV
K
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