ID   A8AUC6_STRGC            Unreviewed;      1472 AA.
AC   A8AUC6;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ABV09503.1};
GN   OrderedLocusNames=SGO_0064 {ECO:0000313|EMBL:ABV09503.1};
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09503.1, ECO:0000313|Proteomes:UP000001131};
RN   [1] {ECO:0000313|EMBL:ABV09503.1, ECO:0000313|Proteomes:UP000001131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC   {ECO:0000313|Proteomes:UP000001131};
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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DR   EMBL; CP000725; ABV09503.1; -; Genomic_DNA.
DR   RefSeq; WP_011999613.1; NC_009785.1.
DR   STRING; 467705.SGO_0064; -.
DR   KEGG; sgo:SGO_0064; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_003134_2_1_9; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR023839; Firmicutes_EssC_C.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03928; T7_EssCb_Firm; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50901; FTSK; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          642..836
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          988..1174
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         662..669
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1005..1012
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1472 AA;  167799 MW;  F9A86AAACC831F5F CRC64;
     MTKQVIFYTQ GLRYEVEPTE GRQLLLGASE KAQVYLPQQE EEIRLKADGD EIFYQFGEET
     GLLTDGLVLN QIRFCLRDKT PTVYDLLDQQ ELRIGAQSGS SLQISDDLEL LLQKNGENWH
     LTKFKGTFYR NNILEKQDQL QLSFGDELSF GAVTIKIYPD EVWLSGPVQA AKVLSLRGAS
     RYGFYPDYPD YHRSPRIIYR GSEDKMVINP PGKEPGKPND ELLKLIVPPL LMIGVVILIT
     LIQPRGIYIL ATMAMSAASI VFSVRTFFKN RKKYKADKKE RVDLYRLYLK DKAIELTDLE
     RKQRQGMLYH FPKVEELTEL TQRYSHRIYE KTPLHFDFLT YRLGLGQVPT SYQLTYGQQE
     RSGKKDALEE EGFALYTKHK KIPDLPIVAN LSHGPVGYVG PRNLVLEQLQ LLVMQLSVFH
     SYHDVQFITI MPEEERDQWN WMRWLPHASL QEMNVRGFVY NQRTRDQVLN SLNQILKLCK
     TQRDEASRQE TTLFSPHYVV LITDEKLILD HVIMEFFTED PTELGCSLLF VEDVMSSLSE
     NVKTVINIKD RNIGQLVMEE GILKETNFRL DHFPDGYDKE QIARTLAPLN HLQNLKSSIP
     DTVTFMEMYG AESFADLKVL DRWKSHAPYK SLAVPIGLRG KDDLVQLNLH EKAHGPHGLI
     AGTTGSGKSE TIQSYILSLA VNFHPHDVGF LLIDYKGGGM AHLFKKLPHL LGTITNLDGA
     QSMRALVSIN AELKRRQRLF NRYEVNHINQ YQKKFKNGEA KEPLPHLFLI SDEFAELKVN
     QPDFMKELVS TARVGRSLGV HLILATQKPS GVVDDQIWSN SRFKLALKVA DRSDSMEMLH
     TPDAAEITQA GRAYLQVGNN EVYELFQSAW SGADYQPDKD ELGIEDHTIY RINDLGQYEV
     LNQDLSGLDL ADEIKEVPTE LDAIVENIQL LAENQEIAPL PQPWLPPLRE RMTLDELEAV
     DFHKEWNKKP SDLELLIGMA DIPQAQKQEP VSINLSKDGN ILLYGSPGTG KTAFLQSAAM
     DLARKYSPKD VTLYLMDFGT NGLAPLSHLP HVADTLLLDQ TEKVAKFVRI MERELNRRKK
     LLSDYGVGTI DLYRQASGQE EPTIVILLDS YEAMKEEPFE AELFKILMRI SREGLSIGVH
     LIMTAGRQSN LRATLYANFK HQMTLKQNDV GEVRTILGST PLAATMEDIK GRILMKRDEV
     DVVQLALPVA GISDAQVINN LRTEVARIQE AWTGETPQAI PMVPEELTEK DFYGREDVVA
     LLDEGKVPLG LDLEKVQPLS WDLIKGNLLY IFEQEWQKIN IINTMLLSFE KLNFDSILLT
     TSKSQKQYRI SKEIGSQLLR ENTIEEIYDL ICENIDLDEI LPRPMVIIWD EIGDLIQENE
     IVSAKILYIM TNGPKVKVYS FITTLPMLSN SLNVVSKFIK QLKYAVVELR LNDQKIISVS
     NVKYSEPALK KSVAYMVDGN HYQAMKLVKG VE
//