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Database: UniProt
Entry: B9KHU0_ANAMF
LinkDB: B9KHU0_ANAMF
Original site: B9KHU0_ANAMF 
ID   B9KHU0_ANAMF            Unreviewed;       210 AA.
AC   B9KHU0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Major surface protein 5 (MSP5) {ECO:0000313|EMBL:ACM49052.1};
GN   Name=msp5 {ECO:0000313|EMBL:ACM49052.1};
GN   OrderedLocusNames=AMF_171 {ECO:0000313|EMBL:ACM49052.1};
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483 {ECO:0000313|EMBL:ACM49052.1, ECO:0000313|Proteomes:UP000007307};
RN   [1] {ECO:0000313|EMBL:ACM49052.1, ECO:0000313|Proteomes:UP000007307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida {ECO:0000313|EMBL:ACM49052.1,
RC   ECO:0000313|Proteomes:UP000007307};
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(2009).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP001079; ACM49052.1; -; Genomic_DNA.
DR   RefSeq; WP_010263025.1; NZ_AFMS01000004.1.
DR   AlphaFoldDB; B9KHU0; -.
DR   SMR; B9KHU0; -.
DR   STRING; 320483.AMF_171; -.
DR   GeneID; 7398627; -.
DR   KEGG; amf:AMF_171; -.
DR   PATRIC; fig|320483.3.peg.198; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_3_1_5; -.
DR   Proteomes; UP000007307; 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   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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007307}.
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         168
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        82..86
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  23132 MW;  7B108E9F2E2EF0FF CRC64;
     MRIFKIVSNL LLFVAAVFLG YSYVNKKGIF SKIGERFTTS EVVSEGIASA SFNNLVNHEG
     VTVSSGDFGG KHMLVIFGFS ACKYTCPTEL GMASQLLSKL GDHADKLQVV FITVDPKNDT
     VAKLKEYHKS FDARIQMLTG EEADIKSVVE NYKVYVGDKK PSDGDIDHST FMYLINGKGR
     YVGHFAPDFN ASEGQGEELF KFVSGHMLNS
//
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