ID   ABP_STRMK               Reviewed;         274 AA.
AC   B2FKA7;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Actin-binding protein Smlt3054 {ECO:0000303|Ref.2};
DE   AltName: Full=Ankyrin repeat protein {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Smlt3054 {ECO:0000312|EMBL:CAQ46503.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND SUBUNIT.
RC   STRAIN=K279a;
RX   DOI=10.1021/acsinfecdis.5b00103;
RA   MacDonald L.C., O'Keefe S., Parnes M.-F., MacDonald H., Stretz L.,
RA   Templer S.J., Wong E.L., Berger B.W.;
RT   "A secreted ankyrin-repeat protein from clinical Stenotrophomonas
RT   maltophilia isolates disrupts actin cytoskeletal structure.";
RL   ACS Infect. Dis. 2:62-70(2016).
CC   -!- FUNCTION: Directly binds F-actin, which results in thickened and
CC       distorted F-actin fibers, and affects cellular F-actin localization.
CC       Thus, may be a host effector whose function is to disrupt host actin
CC       cytoskeletal structure, which may enhance invasion.
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Exists as a dimer as well as a higher order oligomer.
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. Periplasm
CC       {ECO:0000269|Ref.2}.
CC   -!- INDUCTION: Expressed in S.maltophilia clinical isolate K279a grown
CC       under standard conditions (at protein level). {ECO:0000269|Ref.2}.
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DR   EMBL; AM743169; CAQ46503.1; -; Genomic_DNA.
DR   RefSeq; WP_012480684.1; NC_010943.1.
DR   AlphaFoldDB; B2FKA7; -.
DR   SMR; B2FKA7; -.
DR   STRING; 522373.Smlt3054; -.
DR   EnsemblBacteria; CAQ46503; CAQ46503; Smlt3054.
DR   KEGG; sml:Smlt3054; -.
DR   eggNOG; COG0666; Bacteria.
DR   HOGENOM; CLU_1019075_0_0_6; -.
DR   OrthoDB; 1360387at2; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; ANK repeat; Periplasm; Reference proteome; Repeat; Secreted.
FT   CHAIN           1..274
FT                   /note="Actin-binding protein Smlt3054"
FT                   /id="PRO_0000435902"
FT   REPEAT          192..221
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          225..254
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REGION          251..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  29849 MW;  2D1B043D0E23BA9A CRC64;
     MEMDIQESLL RLLRPLGLQR AEALAGALAR EAGASKGLHD SQVLARAHAL SVAPVEGRLG
     DLVWQVRQRE HDGAPQVDLR WGLHRLGLDA PSRASTRDLV RAYERRLADR NEPMVYSTLA
     ERVAGSMAEH TSLFQGMAMA VEEARARRSD ANRLRENAPW QGWLVGASRA GHEAALLACI
     GMGADARLPD ASGNTPLHHA ARFGHFSLVT PLVEAGADVA ALNAHGWAPL HLAALHKHAR
     ACLHLMAHGA NPEQPGWRGR TPTRMHRHEQ TQAL