ID   F2RLN4_STRVP            Unreviewed;       581 AA.
AC   F2RLN4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Protein-lysine 6-oxidase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SVEN_7128 {ECO:0000313|EMBL:CCA60414.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA60414.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA60414.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA60414.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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DR   EMBL; FR845719; CCA60414.1; -; Genomic_DNA.
DR   RefSeq; WP_015038309.1; NZ_JABVZO010000219.1.
DR   AlphaFoldDB; F2RLN4; -.
DR   STRING; 953739.SVEN_7128; -.
DR   GeneID; 69869108; -.
DR   KEGG; sve:SVEN_7128; -.
DR   PATRIC; fig|953739.5.peg.2345; -.
DR   eggNOG; ENOG50333PP; Bacteria.
DR   HOGENOM; CLU_523416_0_0_11; -.
DR   OrthoDB; 914406at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001695; Lysyl_oxidase.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF01186; Lysyl_oxidase; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..581
FT                   /note="Protein-lysine 6-oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039053308"
FT   REGION          233..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  61292 MW;  4825AA852F9AD88D CRC64;
     MTTTRTTRLR RPLLAGTTAV AAMAVTAGFM AATPEQATAA TGPRLSLIAA TDSVTLTSWK
     EEPGVFLDLG TYLTAEGTPL ELKVTRKSYK DPVVVTQTVY EGGKAKAKVL PQNTVKDFSG
     LPGFAEITVT DSTGKKVVSR TESFCPNNAS GRVRPDAPAT SKYPESCPTN PFTLGSVWGV
     EKGWAANTYS GAYTQPVKLA AGTYTAKVGV AKKYRDLFGI ADKPATVRVT VQERSWEDGG
     GAAARQTAGE HAGHGAGQQA PAAHAGHGPG HAPSPAQAGA PETSGAGPSY NVGHGPLKAA
     PPALPWALKR QEAARAEARA ADTTGQTDGS RKAPALTPQA KRPTGTPSVP NVPKPDLRSL
     PAYGITISDG GQDVPGKDYL AFSANVWNAG PAQLVVDGFR SPGKPTMDAF QYFYDANGKQ
     VGYTPTGTME WDPRPGHVHW HFTDFASYRL LKADQKEAVR SGKEAFCLAN TDAVDYTVKN
     ANWHPFNTDL STACGQENSI SVREVLDVGS GDTYTQDLPG QSFDITDVPN GTYYIQVLAN
     PAKRLKETNL DNNSALRKIV LGGTPGKRTV TVPAHDLVNA N
//