ID Q2GDL2_NEOSM Unreviewed; 186 AA.
AC Q2GDL2;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Major surface protein {ECO:0000313|EMBL:ABD46455.1};
GN OrderedLocusNames=NSE_0551 {ECO:0000313|EMBL:ABD46455.1};
OS Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS sennetsu).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=222891 {ECO:0000313|EMBL:ABD46455.1, ECO:0000313|Proteomes:UP000001942};
RN [1] {ECO:0000313|EMBL:ABD46455.1, ECO:0000313|Proteomes:UP000001942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-367 / Miyayama {ECO:0000313|Proteomes:UP000001942};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP000237; ABD46455.1; -; Genomic_DNA.
DR RefSeq; WP_011451940.1; NC_007798.1.
DR AlphaFoldDB; Q2GDL2; -.
DR STRING; 222891.NSE_0551; -.
DR KEGG; nse:NSE_0551; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_1_5; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000001942; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1}.
FT DOMAIN 33..186
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 71
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 71..75
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 186 AA; 21049 MW; 28FD60BE2226ADE2 CRC64;
MINKIVFVFK LLSVALLFGI SYQAEGFNKE ITTSQIDIGG TFKLTDQNGD QVTNNILKGK
YTLVLFGFSR CPHICPGQLT LLEKTLDAFP KLQALFITLD PANDTVEVLN KFSRSFHKRI
LMLTGPNEMI EKIANDYKVY VAANEDPDKF NHSALMYLMG LDGRYISHIA PRSEDELLAF
IYHHTI
//
