ID C4ZCP4_AGARV Unreviewed; 1390 AA.
AC C4ZCP4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ACR74399.1};
GN OrderedLocusNames=EUBREC_0609 {ECO:0000313|EMBL:ACR74399.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR74399.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR74399.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; CP001107; ACR74399.1; -; Genomic_DNA.
DR STRING; 515619.EUBREC_0609; -.
DR PaxDb; 515619-EUBREC_0609; -.
DR KEGG; ere:EUBREC_0609; -.
DR HOGENOM; CLU_003134_2_1_9; -.
DR Proteomes; UP000001477; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00060; FHA; 1.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 2.60.200.20; -; 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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR NCBIfam; TIGR03928; T7_EssCb_Firm; 1.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 565..759
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 898..1081
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 585..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 914..921
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1390 AA; 157509 MW; B2C3807A6537818F CRC64;
MKMENYGWSI ELNPGYVLII GNAPDAHIQL DSAYGRAVRV GLQVKDDISC AMLSEYSSSY
NTLVNGKSIQ RIATVKNHDF ISIGDFTAYY NNGKIFFDYG AIRTNGVEVR PESLDIHTTY
PVFIRNTRIQ AKRDKTPIEI LDPGTIPTKP ELNLVTSLMP SIIMFALVVL LRGVMSKSNG
AFVAFSICSM GVGVFTSIFG IINKQKKYKK DLVKRRDTYL EYIAKKRNEI EAARREELDC
LNAQYYSIEQ DIEHIENFDP VLFDRISTDE DFLEVYLGRG NVESLRQVDY KKQEKLEVGD
DLSSLPEHVA GEYMDIEKAP VVMSLKDANA VGVVGDADSL YSMMKNMIMD IISRQYYGDI
CIYALLDDNI GKYNWLRGIK ALNSSNGNRN IVCDQESKNR VFENLYKELS IRKDEKVHGR
FNIIIVMQDY GIKSHPISKF IEHASELDTV FIFFESKLSL LPLYCSRIID IFDNESAMIY
DSVNKTQKKY FEYENIPDWR VQKAVSILEP VECEEISLAG SLRKNISLFE LLGINSVQAL
NLKERWNSSK IYETMAVPLG VNVKDEIVYL NLHEKFHGPH GLVAGTTGSG KSEILQTFIL
GAATLFHPYE IGFVIIDFKG GGMVNQFRKL PHLIGAITNI DGKAIDRSLR SIKAELLKRQ
NLFAQLNVNH IDKYIKAYKE GQAKVALPHL VIIVDEFAEL KAEQPEFMKE LISAARIGRS
LGVHLILATQ KPAGQVNDQI WSNSKFKLCL KVQTQEDSNE VLKSPLAAEI KEPGRAYLQV
GNNEIFELFQ SGYSGSPESI NGEDDTPFDI YELDFSGKKN LVYKHKLENS EQSRSQLEAV
VEYVDKYCKA DGVKKLPDIC LPALEEVIVY DAELAHNDTP LSMTAVIGIY DDPDRQRQGR
TVIEIGNKNT IIIGASQFGK TNLLELIVRN LAENYSPEEL SIYIIDFASM VLKNFEKLAH
VGGVVCPSDD ERLKNLFKYL SEQIEERRER LLEAGVSSYT SYREAGFTDI PQIVVLIDNY
TALKELYLQD SDILLNLCRE GGSVGISFII SNLQTTGLGY KYLANFSGRI AMFCNESSEY
MTLYGSCKLR PDETAGRCLT EIDGEIYECQ TFLAFEGTKE IERVNNMHAF VDQINAVYGD
ITADKIPEIP ELLTPDYVDH TFRRKNDENI IGIAYDTVAP VYTDHNKCNI ITISGADNMG
RTNFIKYFAL QMLNSEIDTH IYIADDFRRK LSDIGQENVS YDLDPDEFIQ KIIMIEVLLE
EKYKRLIHQE NPEKENTLII INSQEVYTAI SDSKDALNAL KNIMGKYKVL NVYLLFGAVP
NAQIAYGSPD IYKMMKETKS ILFFDNLDNC KIVDIPLAIK RKNQKKIEPG DAYYIFEDEV
SKVRIPLVSD
//