LODA_MARM1
ID LODA_MARM1 Reviewed; 726 AA.
AC F2JXJ3; Q24K54;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=L-lysine 6-oxidase;
DE EC=1.4.3.20;
DE AltName: Full=L-lysine-epsilon-oxidase;
DE AltName: Full=Marinocine;
GN Name=lodA; OrderedLocusNames=Marme_2662;
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=16547036; DOI=10.1128/jb.188.7.2493-2501.2006;
RA Lucas-Elio P., Gomez D., Solano F., Sanchez-Amat A.;
RT "The antimicrobial activity of marinocine, synthesized by Marinomonas
RT mediterranea, is due to hydrogen peroxide generated by its lysine oxidase
RT activity.";
RL J. Bacteriol. 188:2493-2501(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=15652194; DOI=10.1016/j.bbagen.2004.11.002;
RA Lucas-Elio P., Hernandez P., Sanchez-Amat A., Solano F.;
RT "Purification and partial characterization of marinocine, a new broad-
RT spectrum antibacterial protein produced by Marinomonas mediterranea.";
RL Biochim. Biophys. Acta 1721:193-203(2005).
RN [4]
RP CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=17030025; DOI=10.1016/j.bbapap.2006.08.014;
RA Gomez D., Lucas-Elio P., Sanchez-Amat A., Solano F.;
RT "A novel type of lysine oxidase: L-lysine-epsilon-oxidase.";
RL Biochim. Biophys. Acta 1764:1577-1585(2006).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=18502869; DOI=10.1128/jb.00549-08;
RA Mai-Prochnow A., Lucas-Elio P., Egan S., Thomas T., Webb J.S.,
RA Sanchez-Amat A., Kjelleberg S.;
RT "Hydrogen peroxide linked to lysine oxidase activity facilitates biofilm
RT differentiation and dispersal in several gram-negative bacteria.";
RL J. Bacteriol. 190:5493-5501(2008).
RN [6]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX PubMed=20025674; DOI=10.1111/j.1365-2958.2009.07000.x;
RA Gomez D., Lucas-Elio P., Solano F., Sanchez-Amat A.;
RT "Both genes in the Marinomonas mediterranea lodAB operon are required for
RT the expression of the antimicrobial protein lysine oxidase.";
RL Mol. Microbiol. 75:462-473(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH SULFATE AND
RP COFACTOR.
RX PubMed=23908359; DOI=10.1093/jb/mvt070;
RA Okazaki S., Nakano S., Matsui D., Akaji S., Inagaki K., Asano Y.;
RT "X-ray crystallographic evidence for the presence of the cysteine
RT tryptophylquinone cofactor in L-lysine epsilon-oxidase from Marinomonas
RT mediterranea.";
RL J. Biochem. 154:233-236(2013).
CC -!- FUNCTION: Has antibacterial activity against a wide spectrum of Gram-
CC positive and Gram-negative bacteria including nosocomial isolates of
CC S.aureus and Pseudomonas sp. The antimicrobial activity is due to
CC hydrogen peroxide generated by its lysine oxidase activity. Also has
CC autotoxic activity. Involved in biofilm differentiation; responsible
CC for cell death within microcolonies during biofilm development which is
CC linked to the generation of a phenotypically diverse dispersal
CC population and thus may play a role in colonization.
CC {ECO:0000269|PubMed:15652194, ECO:0000269|PubMed:18502869,
CC ECO:0000269|PubMed:20025674}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:22548, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58321; EC=1.4.3.20;
CC Evidence={ECO:0000269|PubMed:16547036, ECO:0000269|PubMed:17030025};
CC -!- COFACTOR:
CC Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252;
CC Evidence={ECO:0000269|PubMed:17030025, ECO:0000269|PubMed:20025674};
CC Note=Contains 1 cysteine tryptophylquinone per subunit.
CC {ECO:0000269|PubMed:17030025, ECO:0000269|PubMed:20025674};
CC -!- ACTIVITY REGULATION: Inhibited by aminoguanidine, amiloride and beta-
CC aminopropionitrile. {ECO:0000269|PubMed:17030025}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for L-lysine;
CC Note=Also uses N(2)-acetyl-L-lysine as substrate.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23908359}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652194,
CC ECO:0000269|PubMed:20025674}.
CC -!- INDUCTION: Forms part of an operon with lodB.
CC -!- PTM: The cysteine tryptophylquinone (CTQ) is generated by oxidation of
CC the indole ring of a tryptophan residue to form tryptophylquinone,
CC followed by covalent cross-linking with a cysteine residue.
CC {ECO:0000269|PubMed:23908359}.
CC -!- MISCELLANEOUS: The intracellular stability of LodA is dependent on the
CC presence of LodB protein. {ECO:0000305|PubMed:20025674}.
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DR EMBL; AY968053; AAY33849.1; -; Genomic_DNA.
DR EMBL; CP002583; ADZ91893.1; -; Genomic_DNA.
DR RefSeq; WP_013661796.1; NC_015276.1.
DR PDB; 2YMW; X-ray; 2.41 A; A/B=1-726.
DR PDB; 3WEU; X-ray; 1.93 A; A/B=1-726.
DR PDB; 3WEV; X-ray; 1.98 A; A/B=1-726.
DR PDBsum; 2YMW; -.
DR PDBsum; 3WEU; -.
DR PDBsum; 3WEV; -.
DR AlphaFoldDB; F2JXJ3; -.
DR SMR; F2JXJ3; -.
DR STRING; 717774.Marme_2662; -.
DR EnsemblBacteria; ADZ91893; ADZ91893; Marme_2662.
DR KEGG; mme:Marme_2662; -.
DR PATRIC; fig|717774.3.peg.2748; -.
DR eggNOG; ENOG502Z8IE; Bacteria.
DR HOGENOM; CLU_012035_1_0_6; -.
DR OMA; PERDECE; -.
DR OrthoDB; 1584770at2; -.
DR BioCyc; MetaCyc:MON-15838; -.
DR BRENDA; 1.4.3.20; 9077.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0033736; F:L-lysine 6-oxidase activity; IDA:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:1900191; P:negative regulation of single-species biofilm formation; IDA:UniProtKB.
DR CDD; cd14732; LodA; 1.
DR InterPro; IPR033797; LodA.
DR InterPro; IPR041173; LodA_C.
DR InterPro; IPR041168; LodA_N.
DR Pfam; PF18417; LodA_C; 1.
DR Pfam; PF17990; LodA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; CTQ; Direct protein sequencing;
KW Oxidoreductase; Quinone; Reference proteome; Secreted; Thioether bond.
FT CHAIN 1..726
FT /note="L-lysine 6-oxidase"
FT /id="PRO_0000418617"
FT MOD_RES 581
FT /note="Tryptophylquinone"
FT CROSSLNK 516..581
FT /note="4'-cysteinyl-tryptophylquinone (Cys-Trp)"
FT CONFLICT 1
FT /note="M -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2YMW"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2YMW"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 237..248
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 407..418
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3WEV"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 498..504
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 529..543
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 557..571
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 596..602
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 612..615
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 619..625
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:3WEU"
FT TURN 635..638
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 662..666
FT /evidence="ECO:0007829|PDB:3WEU"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:3WEU"
FT STRAND 674..680
FT /evidence="ECO:0007829|PDB:3WEU"
SQ SEQUENCE 726 AA; 80880 MW; 1A4E258ADF6B6F1F CRC64;
MALSVHPSIG VARLGNANTD NFVLNPMEIG GLPYEHDVDL KPTTTVVNFK DEAGCIRRQG
QVFKVFGASN EELTLDSPNV KNIEWTVHLA NKKAAWYEFR ELNGNLLYGR DNSYSARGVP
WRNASKTASS ERQSLIIDLG PRSVSGVMAT VEISINNIPE TYLHPSYPSG ELLQGSKHFE
SLGTLRTDSQ GRLIVLGGYG FAGGNTDLSG YGGGDDWYDD ISDGSVTCVV TYSDDSSETS
TAWMVVGSPD FAPEIVNIST LSDTCFDVGV RNFDLVPDMY DSATGHYKSD YVANFDRDIL
PIIQRISQYQ WVSNVQSMSG FFSFQFDYRD GSAANKANRM KYYNYFRQLD NKVIGDYDQP
QQVLMSSEVE GDILPLMPMN SGSNSVSSSN FYDLTDNVVE KFLALDATQL FLLGQWAEGE
FTAGPADDYP VSDMDTASIG NCVGLPMCPG IEMTWSLQNP VIYKDAYQIK HYQDKAYFDV
NGLTPERDEC EEETGCEPGD LTKRMACPWQ ADFFNCTIQT VNFSEPSVNK ASQTETVTSR
THYEWGNLPA GVSVPDQSSV SATKNVDEKV PLPPAYYSYW WPPQSPWDVL TGELDTEGQL
HSHLPAGQQI NYARGINSYS QMVEHWSALA FIRDRNQNND GFPFFTETER NHELFDFKEV
LVGQVTGNSE DNETSLPVFF INANKESLEG KGTKKGKLMA SYFEERAFSK VRSSNIRPRS
GTRMRG
