ID OSPC_BORBU Reviewed; 210 AA. AC Q07337; Q9S3P3; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 127. DE RecName: Full=Outer surface protein C {ECO:0000303|PubMed:8478108}; DE Short=pC {ECO:0000303|PubMed:8478108}; DE AltName: Full=P23 {ECO:0000303|PubMed:8225587}; DE Flags: Precursor; GN Name=ospC {ECO:0000303|PubMed:8478108}; OrderedLocusNames=BB_B19; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OG Plasmid cp26 {ECO:0000269|PubMed:8478109, ECO:0000269|PubMed:9403685}. OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borreliella. OX NCBI_TaxID=224326; RN [1] {ECO:0000312|EMBL:CAA49306.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IMMUNOGENIC IN MAN. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=8098841; DOI=10.1007/bf00195949; RA Jauris-Heipke S., Fuchs R., Motz M., Preac-Mursic V., Schwab E., Will G., RA Wilske B.; RT "Genetic heterogenity of the genes coding for the outer surface protein C RT (OspC) and the flagellin of Borrelia burgdorferi."; RL Med. Microbiol. Immunol. 182:37-50(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=8478108; DOI=10.1128/iai.61.5.2182-2191.1993; RA Wilske B., Preace-Mursic V., Jauris S., Pradel I., Soutschek E., Schwab E., RA Wanner G.; RT "Immunological and molecular polymorphisms of OspC, an immunodominant major RT outer surface protein of Borrelia burgdorferi."; RL Infect. Immun. 61:2182-2191(1993). RN [3] {ECO:0000312|EMBL:AAA16058.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND IMMUNOGENIC IN RP MAN. RC STRAIN=2591, and ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=8225587; DOI=10.1128/iai.61.12.5097-5105.1993; RA Padula S.J., Sampieri A., Dias F., Szczepanski A., Ryan R.W.; RT "Molecular characterization and expression of p23 (OspC) from a North RT American strain of Borrelia burgdorferi."; RL Infect. Immun. 61:5097-5105(1993). RN [4] {ECO:0000312|EMBL:X69589} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PKa; RX PubMed=7665660; DOI=10.1128/jcm.33.7.1860-1866.1995; RA Jauris-Heipke S., Liegl G., Preac-Mursic V., Roessler D., Schwab E., RA Soutschek E., Will G., Wilske B.; RT "Molecular analysis of genes encoding outer surface protein C (OspC) of RT Borrelia burgdorferi sensu lato: relationship to ospA genotype and evidence RT of lateral gene exchange of ospC."; RL J. Clin. Microbiol. 33:1860-1866(1995). RN [5] {ECO:0000312|EMBL:BAA08457.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=7494039; DOI=10.1128/jcm.33.9.2415-2420.1995; RA Fukunaga M., Hamase A.; RT "Outer surface protein C gene sequence analysis of Borrelia burgdorferi RT sensu lato isolates from Japan."; RL J. Clin. Microbiol. 33:2415-2420(1995). RN [6] {ECO:0000312|EMBL:AAC66329.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; PLASMID=cp26; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). RN [7] {ECO:0000312|EMBL:AAB36995.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-210. RC STRAIN=Ip2; RX PubMed=8709845; DOI=10.1111/j.1365-2958.1995.mmi_18020257.x; RA Livey I., Gibbs C.P., Schuster R., Dorner F.; RT "Evidence for lateral transfer and recombination in OspC variation in Lyme RT disease Borrelia."; RL Mol. Microbiol. 18:257-269(1995). RN [8] RP ENCODED ON PLASMID CP26. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; PLASMID=cp26; RX PubMed=8478109; DOI=10.1128/iai.61.5.2192-2195.1993; RA Sadziene A., Wilske B., Ferdows M.S., Barbour A.G.; RT "The cryptic ospC gene of Borrelia burgdorferi B31 is located on a circular RT plasmid."; RL Infect. Immun. 61:2192-2195(1993). RN [9] RP INDUCTION. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31, and JD1; RX PubMed=7708747; DOI=10.1073/pnas.92.7.2909; RA Schwan T.G., Piesman J., Golde W.T., Dolan M.C., Rosa P.A.; RT "Induction of an outer surface protein on Borrelia burgdorferi during tick RT feeding."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2909-2913(1995). RN [10] RP INDCTION IN INFECTED MICE. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=11854355; DOI=10.1084/jem.20011870; RA Liang F.T., Jacobs M.B., Bowers L.C., Philipp M.T.; RT "An immune evasion mechanism for spirochetal persistence in Lyme RT borreliosis."; RL J. Exp. Med. 195:415-422(2002). RN [11] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; PLASMID=cp26; RX PubMed=14970347; DOI=10.1073/pnas.0306845101; RA Grimm D., Tilly K., Byram R., Stewart P.E., Krum J.G., Bueschel D.M., RA Schwan T.G., Policastro P.F., Elias A.F., Rosa P.A.; RT "Outer-surface protein C of the Lyme disease spirochete: a protein induced RT in ticks for infection of mammals."; RL Proc. Natl. Acad. Sci. U.S.A. 101:3142-3147(2004). RN [12] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; PLASMID=cp26; RX PubMed=16714588; DOI=10.1128/iai.01950-05; RA Tilly K., Krum J.G., Bestor A., Jewett M.W., Grimm D., Bueschel D., RA Byram R., Dorward D., Vanraden M.J., Stewart P., Rosa P.; RT "Borrelia burgdorferi OspC protein required exclusively in a crucial early RT stage of mammalian infection."; RL Infect. Immun. 74:3554-3564(2006). RN [13] RP INTERACTION WITH I.RICINUS IRIC-1, AND PROTECTS AGAINST MAMMALIAN IMMUNE RP SYSTEM. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=18752445; DOI=10.1086/591917; RA Hovius J.W., Schuijt T.J., de Groot K.A., Roelofs J.J., Oei G.A., RA Marquart J.A., de Beer R., van 't Veer C., van der Poll T., Ramamoorthi N., RA Fikrig E., van Dam A.P.; RT "Preferential protection of Borrelia burgdorferi sensu stricto by a Salp15 RT homologue in Ixodes ricinus saliva."; RL J. Infect. Dis. 198:1189-1197(2008). RN [14] RP FUNCTION, SUBUNIT, INTERACTION WITH HUMAN PLASMINOGEN, SUBCELLULAR RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-60; 61-GLU--GLU-63; RP GLU-61 AND GLU-63. RC STRAIN=B31-5A4; PLASMID=cp26; RX PubMed=20199597; DOI=10.1111/j.1365-2958.2010.07103.x; RA Earnhart C.G., Leblanc D.V., Alix K.E., Desrosiers D.C., Radolf J.D., RA Marconi R.T.; RT "Identification of residues within ligand-binding domain 1 (LBD1) of the RT Borrelia burgdorferi OspC protein required for function in the mammalian RT environment."; RL Mol. Microbiol. 76:393-408(2010). RN [15] RP FUNCTION AS A PLASMINOGEN RECEPTOR, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=22433849; DOI=10.1074/jbc.m111.290775; RA Oender O., Humphrey P.T., McOmber B., Korobova F., Francella N., RA Greenbaum D.C., Brisson D.; RT "OspC is potent plasminogen receptor on surface of Borrelia burgdorferi."; RL J. Biol. Chem. 287:16860-16868(2012). RN [16] RP FUNCTION IN INHIBITING PHAGOCYTOSIS BY HOST MACROPHAGES, AND DISRUPTION RP PHENOTYPE. RC STRAIN=297, and ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=26438793; DOI=10.1128/iai.01215-15; RA Carrasco S.E., Troxell B., Yang Y., Brandt S.L., Li H., Sandusky G.E., RA Condon K.W., Serezani C.H., Yang X.F.; RT "Outer surface protein OspC is an antiphagocytic factor that protects RT Borrelia burgdorferi from phagocytosis by macrophages."; RL Infect. Immun. 83:4848-4860(2015). RN [17] RP FUNCTION, AND INDUCTION. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31 / ML23; RX PubMed=27611840; DOI=10.1371/journal.pone.0162501; RA Skare J.T., Shaw D.K., Trzeciakowski J.P., Hyde J.A.; RT "In Vivo Imaging Demonstrates That Borrelia burgdorferi ospC Is Uniquely RT Expressed Temporally and Spatially throughout Experimental Infection."; RL PLoS ONE 11:e0162501-e0162501(2016). RN [18] RP FUNCTION, INTERACTION WITH HUMAN C4B, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=28873507; DOI=10.1111/cmi.12786; RA Caine J.A., Lin Y.P., Kessler J.R., Sato H., Leong J.M., Coburn J.; RT "Borrelia burgdorferi outer surface protein C (OspC) binds complement RT component C4b and confers bloodstream survival."; RL Cell. Microbiol. 19:0-0(2017). RN [19] RP ERRATUM OF PUBMED:28873507. RX PubMed=33285028; DOI=10.1111/cmi.13286; RA Caine J.A., Lin Y.P., Kessler J.R., Sato H., Leong J.M., Coburn J.; RT "Corrigendum."; RL Cell. Microbiol. 23:e13286-e13286(2021). RN [20] {ECO:0000312|PDB:1GGQ} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 44-200, AND SUBUNIT. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=11230121; DOI=10.1093/emboj/20.5.971; RA Kumaran D., Eswaramoorthy S., Luft B.J., Koide S., Dunn J.J., Lawson C.L., RA Swaminathan S.; RT "Crystal structure of outer surface protein C (OspC) from the Lyme disease RT spirochete, Borrelia burgdorferi."; RL EMBO J. 20:971-978(2001). CC -!- FUNCTION: A major immunodominant protein in mammalian hosts CC (PubMed:8098841, PubMed:8478109, PubMed:8225587). Required for the CC initial stages of mammalian infection (PubMed:14970347, CC PubMed:16714588, PubMed:20199597, PubMed:28873507). Interaction with CC tick I.ricinus salivary protein Salp15 protects the bacteria from CC antibody-mediated killing in vitro and in vivo (PubMed:18752445). CC Inhibits macrophage-mediated phagocytosis of the bacteria CC (PubMed:26438793). Binds human plasminogen; this probably confers an CC extracellular protease activity on the bacteria that allows it to CC traverse tissue (PubMed:20199597, PubMed:22433849). Binds human CC complement C4-B, which may inhibit the complement cascade CC (PubMed:28873507) (Probable). Experiments in mice suggest it may play CC another role after initial infection (PubMed:27611840) (Probable). CC {ECO:0000269|PubMed:14970347, ECO:0000269|PubMed:16714588, CC ECO:0000269|PubMed:18752445, ECO:0000269|PubMed:20199597, CC ECO:0000269|PubMed:22433849, ECO:0000269|PubMed:26438793, CC ECO:0000269|PubMed:28873507, ECO:0000269|PubMed:8098841, CC ECO:0000269|PubMed:8225587, ECO:0000269|PubMed:8478109, CC ECO:0000305|PubMed:27611840, ECO:0000305|PubMed:28873507}. CC -!- SUBUNIT: Homodimer (PubMed:20199597, PubMed:11230121). Binds human CC plasminogen on the bacterial surface, also binds human plasmin CC (PubMed:20199597, PubMed:22433849). Interacts with tick I.ricinus CC salivary protein Iric-1 (PubMed:18752445). Interacts with human CC complement C4 beta chain (C4B); whole bacteria bind to wells coated CC with C4b. Binding is inhibited by human complement factor C2 CC (PubMed:28873507). {ECO:0000269|PubMed:11230121, CC ECO:0000269|PubMed:18752445, ECO:0000269|PubMed:20199597, CC ECO:0000269|PubMed:22433849, ECO:0000269|PubMed:28873507}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. Cell surface CC {ECO:0000269|PubMed:20199597, ECO:0000269|PubMed:22433849, CC ECO:0000269|PubMed:28873507, ECO:0000269|PubMed:8225587}. CC Note=Expressed in a punctate fashion on a subset of cells in vitro. CC {ECO:0000269|PubMed:22433849}. CC -!- INDUCTION: Expressed variably in vitro in strain B31; detected in CC immunocompetent infected mice at 10 days post-infection but not after CC 17 days (PubMed:11854355). Not expressed in the tick midgut of unfed CC ticks, expressed in tick midgut following feeding on mice (at protein CC level). The change in expression is at least partially due to a CC temperature shift, expressed in vitro at 37 but not 24 degrees Celsius CC (at protein level) (PubMed:7708747). More highly expressed at pH 7.0 CC than pH 8.0 in vitro (at protein level) (PubMed:14970347). Transcripts CC are most abundant 7 days post-infection in infected mice, but continue CC to be expressed for at least 21 days. They are found at varying levels CC in the tissues tested (heart, inguinal lymph node, bladder, tibiotarsal CC joint and skin at the injection site) where they vary over the course CC of the experiment (PubMed:27611840). {ECO:0000269|PubMed:11854355, CC ECO:0000269|PubMed:14970347, ECO:0000269|PubMed:27611840, CC ECO:0000269|PubMed:7708747}. CC -!- DISRUPTION PHENOTYPE: No observable effect on growth in vitro, infects CC ticks normally, required to infect mice. No change in ability to CC colonize the tick midgut, no change in bacterial migration to the tick CC salivary gland (PubMed:14970347, PubMed:16714588). Loss of infectivity CC in mice, including SCID and NOSCIDg mice (deficient in T and B cells, CC functional natural killer (NK) cells which also lack complement C5) CC (PubMed:20199597, PubMed:26438793). About 40-70% more uptake by murine CC peritoneal macrophages and human macrophages (B.burgdorferi strains B31 CC and 297 deleted); no change in uptake by neutrophils (PubMed:26438793). CC Whole bacteria no longer interact with human plasminogen CC (PubMed:22433849). Only about 12% of bacteria survive in mouse CC bloodstream longer than 30 minutes post-inoculation, decreased CC bacterial binding to C4b in vitro (PubMed:28873507). CC {ECO:0000269|PubMed:14970347, ECO:0000269|PubMed:16714588, CC ECO:0000269|PubMed:20199597, ECO:0000269|PubMed:22433849, CC ECO:0000269|PubMed:26438793, ECO:0000269|PubMed:28873507}. CC -!- MISCELLANEOUS: The causative agent of Lyme disease, the bacteria has an CC enzootic lifestyle. Larval ticks are infected with bacteria during CC feeding on infected hosts (mostly mammals) which retain the bacteria CC during subsequent developmental stages. It is transmitted to the next CC host when it is bitten by ticks. During tick feeding (which can last CC for several days), bacterial migrate from the tick midgut to the CC salivary gland where they are transmitted to the host. {ECO:0000305}. CC -!- MISCELLANEOUS: Expression of the mRNA for this protein in infected mice CC occurs in different tissues (including host heart, bladder and joints CC far from the initial injection site) at different levels for at least CC 21 days post-infection, suggesting it may play another role after CC initial infection. {ECO:0000269|PubMed:27611840}. CC -!- SIMILARITY: Belongs to the OspC lipoprotein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X69596; CAA49306.1; -; Genomic_DNA. DR EMBL; U01894; AAA16058.1; -; Unassigned_DNA. DR EMBL; X69589; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D49497; BAA08457.1; -; Genomic_DNA. DR EMBL; AE000792; AAC66329.1; -; Genomic_DNA. DR EMBL; L42887; AAB36995.1; -; Genomic_DNA. DR PIR; G70218; G70218. DR PIR; S69927; S69927. DR RefSeq; NP_047005.1; NC_001903.1. DR RefSeq; WP_010890595.1; NC_001903.1. DR PDB; 1GGQ; X-ray; 2.51 A; A/B/C/D=39-200. DR PDB; 7UIJ; X-ray; 2.70 A; C/D=38-201. DR PDBsum; 1GGQ; -. DR PDBsum; 7UIJ; -. DR AlphaFoldDB; Q07337; -. DR BMRB; Q07337; -. DR SMR; Q07337; -. DR EnsemblBacteria; AAC66329; AAC66329; BB_B19. DR KEGG; bbu:BB_B19; -. DR PATRIC; fig|224326.49.peg.1608; -. DR HOGENOM; CLU_089887_0_0_12; -. DR OrthoDB; 352157at2; -. DR EvolutionaryTrace; Q07337; -. DR Proteomes; UP000001807; Plasmid cp26. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0031240; C:external side of cell outer membrane; IDA:CAFA. DR GO; GO:0016020; C:membrane; IDA:CAFA. DR Gene3D; 1.20.120.240; Lipoprotein, type 6; 1. DR InterPro; IPR001800; Lipoprotein_OspC. DR InterPro; IPR036437; OspC-like_sf. DR Pfam; PF01441; Lipoprotein_6; 1. DR SUPFAM; SSF63515; Outer surface protein C (OspC); 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate; KW Plasmid; Reference proteome; Signal; Virulence. FT SIGNAL 1..18 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 19..210 FT /note="Outer surface protein C" FT /id="PRO_0000018083" FT LIPID 19 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT LIPID 19 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT VARIANT 51 FT /note="D -> E (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 56 FT /note="L -> V (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 64..67 FT /note="ALLS -> TLLA (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 72..93 FT /note="IAAKAIGKKIHQNNGLDTENNH -> VAKKAIGNLIAQNGLNAGANQ (in FT strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 103 FT /note="A -> V (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 109..110 FT /note="KQ -> AE (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 118..119 FT /note="EG -> SEE (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 125..126 FT /note="DA -> ED (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 131..133 FT /note="SET -> NKA (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 136 FT /note="N -> D (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 140..144 FT /note="EKHTD -> SSHAE (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 147..150 FT /note="KEGV -> IANGAA (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 154..157 FT /note="DAKE -> NAKA (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 167 FT /note="T -> D (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 171..174 FT /note="EELG -> QELE (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 181..182 FT /note="EV -> KN (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 188..192 FT /note="KEMLA -> QETLN (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT VARIANT 206 FT /note="S -> N (in strain: 2591)" FT /evidence="ECO:0000269|PubMed:8225587" FT MUTAGEN 60 FT /note="K->Y: Wild-type virulence in mice, no antibody FT response in mice, decreased heart colonization-." FT /evidence="ECO:0000269|PubMed:20199597" FT MUTAGEN 61..63 FT /note="EVE->QVQ: Bacteria are non-infectious in mice, no FT antibody response in mice, increased affinity for human FT plasminogen." FT /evidence="ECO:0000269|PubMed:20199597" FT MUTAGEN 61 FT /note="E->Q: Bacteria are non-infectious in mice, no FT antibody response in mice." FT /evidence="ECO:0000269|PubMed:20199597" FT MUTAGEN 63 FT /note="E->Q: Wild-type virulence in mice, no antibody FT response in mice, colonizes organs like wild-type." FT /evidence="ECO:0000269|PubMed:20199597" FT HELIX 42..75 FT /evidence="ECO:0007829|PDB:1GGQ" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:1GGQ" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:1GGQ" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:1GGQ" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 95..113 FT /evidence="ECO:0007829|PDB:1GGQ" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 121..140 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:1GGQ" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:1GGQ" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 170..195 FT /evidence="ECO:0007829|PDB:1GGQ" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:1GGQ" SQ SEQUENCE 210 AA; 22341 MW; 7A4FC978F91777BF CRC64; MKKNTLSAIL MTLFLFISCN NSGKDGNTSA NSADESVKGP NLTEISKKIT DSNAVLLAVK EVEALLSSID EIAAKAIGKK IHQNNGLDTE NNHNGSLLAG AYAISTLIKQ KLDGLKNEGL KEKIDAAKKC SETFTNKLKE KHTDLGKEGV TDADAKEAIL KTNGTKTKGA EELGKLFESV EVLSKAAKEM LANSVKELTS PVVAESPKKP //