ID C3XH89_9HELI Unreviewed; 1543 AA.
AC C3XH89;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=HRAG_01435 {ECO:0000313|EMBL:EEO24378.2};
OS Helicobacter bilis ATCC 43879.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=613026 {ECO:0000313|EMBL:EEO24378.2, ECO:0000313|Proteomes:UP000005085};
RN [1] {ECO:0000313|EMBL:EEO24378.2, ECO:0000313|Proteomes:UP000005085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43879 {ECO:0000313|EMBL:EEO24378.2,
RC ECO:0000313|Proteomes:UP000005085};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEO24378.2}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACDN02000023; EEO24378.2; -; Genomic_DNA.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_003936_0_0_7; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000005085; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000005085};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1224..1410
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1241..1248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1543 AA; 173976 MW; 139E02AA2971549C CRC64;
MLYLWLATIF GYTPPDAALS GAALTNSFFK IGGFGNSFAN FNRGMFGYLA YIYLPLLLLP
IYRFHDDTSY SFRKIQLSFA YLLLFIGLLL LQSLVFHSGQ FGNYLQEVLT PYIGLFGVAI
LTFICISTAL LLIAERTATF ILGYLGGSLQ MAYSATSNFA KRMFQQLKSK YTDFKLDSIQ
REKRKIVNQE LSEKATTTKS KYIDREPLLE TALDEYPRTN TNNGYTDTNM QNLAKNENLA
HNKNKHSSNT QTTNKQEIPQ DSKEFSIQVK PSNNINTTQT LSYQQYDDSN ISPITHTPRT
QMRNNDEELL KRFQKANLYP KQKDQQAFHT DSPMTFRLKQ EMSEANPLES FAKTQSPKIL
PTIDDWQTTD MPPREVKTTN LIKPKTQERE QPKTETFSVK EGITTQDNAT PTTPKILESF
KEDSTAQIQP KTITQESPTI RIKEPEIKDS TNTHLNTPKP EINPNQQHTE QKKTIKIQAI
NTPKIEQMPT QANYKTLDMS FTQKEYKTTN PSINESTITL SQPNSTDFNQ TTQEITNLNQ
TQITESNLNV AQTLESQHID YTSQQYDLNT QTLQQNTLDS QPSELVLQQD ILETNNLQDS
PFITPLESTQ NNIDYTETTT IIIPPLLDSN EDSRNDFREE FRGDFNTQDL IIQDSISKDT
SINNSQDSII IESIPQESTH SLDSTESNHT LQDDIREEIK EIFIEPLESL EAHTQSISQS
SQIDSKQTDF ISTESNMLNS NKLDTIHIDS IPTESNVSNL NQIESSYTDS IDLLKTNSSI
ESKQAESIPQ DSILIETTQI ESNIQTQHTQ DFEIKEITQE NTEHVENIES SITDSNLTKE
LKNKDYLQQS TMQDLEQHHT DSKIAQEITP AQQNITINTY TPQMTHSHFP THTNPTNYFT
GIPTHSQAQP MNYIFDSTTH TQTSTIKPNV ESSTIESNNQ QFHNTESNLA QPNNTQSNEI
ENNTTQHNLA QSNNIESTHT NLTTQPIKIK LYDDTQASRT ITHKDIMQNN ISTQTKDTAH
SFTIKDSSPH IESKTTQITE SNDHENREDM IIRQIAQKKE EARQESNMLI ANHDTNIANL
AQSTNLPPFI LPPLKLLQEP IAQDSIQDIE LDSKIDKMLQ IFNAHKIRGD IIATLTGPVV
TTFEFRPETH VKVSKILSHK NDLARILKAK SIRIQAPIPG KDVIGIQIPN SKVETIYLRE
ILHSQAFLDS KDPLTIALGK DISGTPIVAN LAKLPHLLVA GTTGSGKSVG VNAIILSLLY
RNDPDNLKLM MIDPKQVEFA PYEDLPHLIT PIINAPNKAI KALQVATIEM DKRYELFSQI
KVKNIASYNE KVSIKMPNFV IIIDELADLM ITGGKEAEAF IARIAQMGRA AGMHLIIATQ
RSSVNVITGH IKANLPSRIS YRVGSRIDSK VILDEMGAED LLGNGDGLFT TTNGLMRIHA
PWVSEQEVEH IVDFIKAQRE PQYDESFLSE TKPGSVSGDK FSGDGSLLDK AKEVMMQDNK
TSISYLQRKL GIGYNKSASL VEALEKEGFL SPPNSKGERN ILV
//
