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Database: UniProt
Entry: C9ZC53_STRSW
LinkDB: C9ZC53_STRSW
Original site: C9ZC53_STRSW 
ID   C9ZC53_STRSW            Unreviewed;       458 AA.
AC   C9ZC53;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative plasmid transfer protein {ECO:0000313|EMBL:CBG71743.1};
GN   Name=traSA {ECO:0000313|EMBL:CBG71743.1};
GN   OrderedLocusNames=SCAB_46901 {ECO:0000313|EMBL:CBG71743.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG71743.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG71743.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG71743.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG71743.1; -; Genomic_DNA.
DR   RefSeq; WP_013002337.1; NC_013929.1.
DR   AlphaFoldDB; C9ZC53; -.
DR   STRING; 680198.SCAB_46901; -.
DR   GeneID; 24311160; -.
DR   KEGG; scb:SCAB_46901; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_633003_0_0_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          170..368
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          434..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         187..194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   458 AA;  49291 MW;  ACB251DC71B86927 CRC64;
     MSDLVTLLEV GGPLAALGGG AAYTRAKHPR VYWPTVGLPI STARLLGSYG SVMEACGLTV
     APSRLRVLAV KATTRREVRP VPPRRGIIRP TSTGLRLRLR LAPGQEPADV AASAERLRHA
     WGVHAVYVTT VKPGVVELRL VGFDVLRNVR MPRKATAELL KVPVALREDA TPFVRDYRTI
     PHQLTLGATL SGKSMYLRHL ITGLAWQPVA LVGIDCKRGV ELAPFASRLS ALATDPDEAA
     ELLPVLIKEM EDRYDLIKAR QGIAPGTPDE EITSDIWGLP DSERPVPIVL FVDEVAELFL
     VATKKDEERR DEMVTQLIRL AQLGRAAGIY LEVCGQRFGA ELGKGATMLR AQLTGRVCHR
     VNDEASAKMA LGDIAPEAVS AACAIAPELP GLAVAGDTSG GWSRIRTPYL SLGAAAEICR
     DTSHLVPDLP ALKPFRPDTP VRPVESSAPA VQPHPVTD
//
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