ID A0A1T3NL72_9ACTN Unreviewed; 1562 AA.
AC A0A1T3NL72;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cell division protein FtsY {ECO:0000313|EMBL:OPC77415.1};
GN ORFNames=B4N89_43700 {ECO:0000313|EMBL:OPC77415.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC77415.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC77415.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC77415.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OPC77415.1}.
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DR EMBL; MWQN01000004; OPC77415.1; -; Genomic_DNA.
DR STRING; 159449.B4N89_43700; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000190037; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:OPC77415.1};
KW Cell division {ECO:0000313|EMBL:OPC77415.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000190037};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 290..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 689..881
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1056..1247
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 154..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 707..714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1074..1081
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1562 AA; 167173 MW; F4BBBBECFF488BF6 CRC64;
MPVNLALTTT DPQGRRSDHL LDVPDSATVA DLGSVLGAAD LFLGDRRLNP DARVGASGIR
PGAVIGLGGP APTETATRAW RPPGSDPVLV TVRHVSGPGA GRVWRLGPGR HEVGTDRACA
LRLDGGGAPA QGTWITVGAD GSVTVALPDD ADEADCGLRS LTPPPPVDPI TGTPLSAEEP
AGTQEGGPGG HSTEPPPTGP DGQPVQPPPP PVGQLPPLDD GSLPWPTYAD LSLGEHLLRP
GPPDEPEAAV RPAPDGLGIE YNRPPRIAPH LDAESIRMMG PPTDTSKRPF PFLMMIAPLL
MGLAMMFLFR SLFFVIFVFF TPLMAVGNWI SGKRTGRRDY QEAKRVYRIR RSALETEMRR
ATVEERGLRN STFPDPAALL LTATGPGLAL WQRRRRDSDH LTIRLGTLTR ASLKSIDDQA
RENHYRNVNW RIADVPFGVE MTAFGVVGIG ASGELPRRIA SWAVIQTAVL HSPRDVRVVV
LTEDEHAEAW QWVRWLPHLR PGRPGAAVVA LGTDPESTAH RVNELISDVQ TRLDSSQSAL
GPTLQREPDV LVILDGARRL RDVPGMIEVL TNGPAVRVFS LCLEEREHLL PEECTAVVTA
NGGRLDLKAS HVPEVKGIRA DLVDPAWCEE VARALAPVLD VTVESDSGLP SEVALLPLIG
QEPPDAEVLL RAWARRPAST TFVLGSGYEG VLRLDLVRDG PHGLIGGTTG SGKSELLQTM
IASLAAVNRP DELTFVLVDY KGGSAFRECA ELPHTLGMIT DLDGHLVKRA LASLDAELRR
RETVLNEVEA KDHTEYRIKR ARDPRLPPLP RLLLVIDEFA TLVRELPDFV PGLISLAQRG
RSLGLHLLLA TQRPGGSVSN EIKANTNLRM ALRVTDRSES QDIIDGIEAA GISANNPGRA
LVRRGEGPPT PFQTAFVGGE RPGAVPSSIA KAAATRPVRG IRLGWQRLGR PLDFSEADAG
ADIENDTDTG PESPFDPHED SMSGQSEELP TDLRALVDAL REAADRLPDF RPQPSPWLPP
MDDRMRLDEL PAIPEPAPGA LPMVPYALLD IPHLQARRLA AIDFASFGHL YVIGAPRSGR
TQVLRTIAGA GALTIPCSDL HIYAIDAAGG GLSVLEALPH CGAVVSRHDA ERMERLINRL
IAELTVRQRL IARHDCADVT ELRGKVGKDQ RPAHLVLMVD GWDALSTMLD DYDGGRLYAD
VVRLLREGQG AGIHVIATSE RLLLGGRLAA HNDHRLLLRQ TDPGDYTLIG IPRNSIPAAV
APGRGWLAPG AIEAQIALLP SIAEAPVAAA VDGDDPSAND QSDQAEAMRE LGRRATVRDS
NVPDVRRPFR VGEMPTLIGF QEAHDRVPQS LRKPFHALLG VGGDAVAPLT YDFADGGGSF
MVAGPPRSGR TTALAAMCVS LLMGGTRLVV LTPRDSQLRK LSAHGLAQVL TDPDPEPEVL
VEALTSVREH PVVVVVDDAD LMLACSADSV LRRIATSGRD HGQGLLLAGL AESMSSLGWV
GMARRSRRGL LLGPKTLGEA DLIGARLSAE QVRTPLGPGR GWTAGDAGAA IAVQVPLTVL
DG
//
