LP49_LEPIC
ID LP49_LEPIC Reviewed; 456 AA.
AC Q72U69;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Antigen Lp49 {ECO:0000303|PubMed:18508281};
DE AltName: Full=Leptospiral 49 kilodalton protein {ECO:0000303|PubMed:17609931};
DE Short=Lp49 {ECO:0000303|PubMed:17609931};
DE Flags: Precursor;
GN Name=orfC {ECO:0000312|EMBL:AAS69409.1};
GN OrderedLocusNames=LIC_10793 {ECO:0000312|EMBL:AAS69409.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671 {ECO:0000312|EMBL:AAS69409.1};
RN [1] {ECO:0000312|EMBL:AAS69409.1, ECO:0000312|Proteomes:UP000007037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130 {ECO:0000312|EMBL:AAS69409.1,
RC ECO:0000312|Proteomes:UP000007037};
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
RN [2]
RP SUBCELLULAR LOCATION, BIOTECHNOLOGY, AND CIRCULAR DICHROISM.
RX PubMed=17609931; DOI=10.1007/s00203-007-0273-2;
RA Neves F.O., Abreu P.A., Vasconcellos S.A., de Morais Z.M., Romero E.C.,
RA Nascimento A.L.;
RT "Identification of a novel potential antigen for early-phase serodiagnosis
RT of leptospirosis.";
RL Arch. Microbiol. 188:523-532(2007).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20582320; DOI=10.1371/journal.pone.0011259;
RA Vieira M.L., Atzingen M.V., Oliveira T.R., Oliveira R., Andrade D.M.,
RA Vasconcellos S.A., Nascimento A.L.;
RT "In vitro identification of novel plasminogen-binding receptors of the
RT pathogen Leptospira interrogans.";
RL PLoS ONE 5:E11259-E11259(2010).
RN [4] {ECO:0007744|PDB:3BWS}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 34-456, AND DISULFIDE BOND.
RX PubMed=18508281; DOI=10.1016/j.jsb.2008.04.003;
RA Giuseppe P.O., Neves F.O., Nascimento A.L., Guimaraes B.G.;
RT "The leptospiral antigen Lp49 is a two-domain protein with putative protein
RT binding function.";
RL J. Struct. Biol. 163:53-60(2008).
CC -!- FUNCTION: May be involved in virulence. Binds human plasminogen (PLG)
CC and stimulates its proteolytic cleavage to enzymatically active plasmin
CC in the presence of an urokinase-type PLG activator in vitro. Activated
CC plasmin has proteolytic activity which may help the bacteria to spread
CC throughout the host by degrading extracellular matrix components,
CC facilitating tissue penetration and invasion.
CC {ECO:0000269|PubMed:20582320}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:17609931,
CC ECO:0000269|PubMed:20582320}.
CC -!- BIOTECHNOLOGY: May be useful for detecting a broad spectrum of
CC Leptospira infection in humans and animals due to its presence in
CC several pathogenic serovars of L.interrogans including copenhageni,
CC canicola, hardjo, icterohaemorrhagiae and pomona, and also in
CC L.borgpetersenii hardjo. May be used for serodiagnosis of both early
CC and convalescent phases of leptospirosis infectious disease.
CC {ECO:0000269|PubMed:17609931}.
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DR EMBL; AE016823; AAS69409.1; -; Genomic_DNA.
DR RefSeq; WP_001087680.1; NC_005823.1.
DR PDB; 3BWS; X-ray; 1.99 A; A/B=34-456.
DR PDBsum; 3BWS; -.
DR AlphaFoldDB; Q72U69; -.
DR SMR; Q72U69; -.
DR PaxDb; Q72U69; -.
DR EnsemblBacteria; AAS69409; AAS69409; LIC_10793.
DR GeneID; 61144129; -.
DR KEGG; lic:LIC_10793; -.
DR HOGENOM; CLU_049724_0_0_12; -.
DR OMA; NWESNDI; -.
DR Proteomes; UP000007037; Chromosome I.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IPI:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR019405; Lactonase_7-beta_prop.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF10282; Lactonase; 1.
DR SUPFAM; SSF50974; SSF50974; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Lipoprotein; Membrane;
KW Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..456
FT /note="Antigen Lp49"
FT /id="PRO_0000436553"
FT DISULFID 346..347
FT /evidence="ECO:0000269|PubMed:18508281,
FT ECO:0007744|PDB:3BWS"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3BWS"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 152..163
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3BWS"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:3BWS"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3BWS"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 233..243
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:3BWS"
FT TURN 443..446
FT /evidence="ECO:0007829|PDB:3BWS"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:3BWS"
SQ SEQUENCE 456 AA; 51845 MW; DE7F87AF87F3B45A CRC64;
MNSNPKKKFL KLIKIKSDII LLIPIFLFLV CCKSGDFSLL SSPINREKNG TEIVKFSIHP
YKGTVIRLGE EILPFKVLEM DKNIALVEMA IPVYKDEKEI ELKLSSPGFQ NSSYRIRKPE
ELNEKLIALD KEGITHRFIS RFKTGFQPKS VRFIDNTRLA IPLLEDEGMD VLDINSGQTV
RLSPPEKYKK KLGFVETISI PEHNELWVSQ MQANAVHVFD LKTLAYKATV DLTGKWSKIL
LYDPIRDLVY CSNWISEDIS VIDRKTKLEI RKTDKIGLPR GLLLSKDGKE LYIAQFSASN
QESGGGRLGI YSMDKEKLID TIGPPGNKRH IVSGNTENKI YVSDMCCSKI EVYDLKEKKV
QKSIPVFDKP NTIALSPDGK YLYVSCRGPN HPTEGYLKKG LVLGKVYVID TTTDTVKEFW
EAGNQPTGLD VSPDNRYLVI SDFLDHQIRV YRRDGF
