ID A0A0Q4HEF7_9MICO Unreviewed; 1503 AA.
AC A0A0Q4HEF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phosphopeptide-binding protein {ECO:0000313|EMBL:KQM84317.1};
GN ORFNames=ASE68_14825 {ECO:0000313|EMBL:KQM84317.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM84317.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM84317.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM84317.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM84317.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM84317.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KQM84317.1}.
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DR EMBL; LMKQ01000001; KQM84317.1; -; Genomic_DNA.
DR RefSeq; WP_055860253.1; NZ_LMKQ01000001.1.
DR STRING; 1735688.ASE68_14825; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000050813; Unassembled WGS sequence.
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; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032030; YscD_cytoplasmic_dom.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF16697; Yop-YscD_cpl; 1.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 122..171
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 696..884
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1023..1214
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT COILED 291..318
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 714..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1040..1047
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1503 AA; 160524 MW; E1A0819C168FAFE7 CRC64;
MKLKVGLRRQ QGAPVDLVIT TDATATVGDV ASAIAHNDPA SPGLRGATGL SLAVAPPTSS
EPVVLDPQVL IGDAAIGSGF NAAVVAGQTA GGQGGQSAVA AVMRVHNGPD AGREFPLPRG
ASIIGRAAGA DIVLVDALAS KRHARVEVDQ ASIELVDLNS ANGLVVDGGL VQRVRVIPGQ
KITIGDTDIS FSLVATGDAA PSSDPVLERG GSLMFNRSPR VEERYPGTEH RHPTVPNEAE
PRLFPWPMIV APIMLGFAMF AFTGRATSLL IVAMSPLMML GNFVGQRTQQ GKKLRLEIDT
FETQIEDLEE RLAKETIVER ARRLEESPAV AAVYEQAMRL GPLLWTRRPE HWNFLALRLG
IGRARSRNTV AQTSELKGIA RYASQVDVLR DRHEFIDDVP LVEMLPSSGA IGIAGPRHLA
ADVLRGLGVQ LFGLHAPNEL VTAAIVDPAW AREIEWMKWL PHTTSPKSPF AELALADSQS
AGTALLNALE ETILERLSGT ASRRGPLSTD DSTMSLGARV GGSGGSAGEL DGDLALVLIA
SNDAPVDRPR LTQVIERGAD AGIFTIFLAP TVESLPAACR TFIDATDGLE HARVGYVRAG
EDYREAVIEG VSNQYAEVFA KRLAPVVDSS SVTADSTDLP RSVSLLRLLG TDMAAQPSTA
VERWRQNNSV LDRTRGTRPR LKRAGTLKAY IGQGSPDAMS LDLRTQGPHA LVGGTTGSGK
SEFLQAWVLG MAAEYSPDRV TFLFVDYKGG SAFADCVELP HCVGLVTDLS PHLVRRALTS
LRAELHHREH LFNRKKAKDL LELEKRQDPE TPPALVLVID EFAALAGEVP EFVDGVVDIA
QRGRSLGIHL IMATQRPAGV IKDNLRANTN LRVALRMADV SDSNDVVGDP IAGTFDPSIP
GRGIAKTGPG RLVPFQSGYA GGWTTDVPDV AQAKVAELRF GGAIVWEGDA EGESDTHDED
LGPNDQKRLV KNLIAAASEA RIPAPRRPWL DDLATTVDLR SLPQDGDSRI PLGLADIPER
QLQEPMYFEP DTDGHMLVYG TSGAGKSTAL RSIALAAGAR PDLARAVVYG LDFGTGSLRA
IEELPHVGSI VPGDDAERVQ RLLRNIRSVL DERAKRFSAV NAATLSEYRA ITGRTDESRI
LLLIDGFGTF KQEWETTSAR SPFYAIFMRL LGEGRPLGIH AIVTADRYGA VPTAVSANVS
KRIILRMSDD GAYAILGAPK DVLNERSAPG RAIVDGFETQ IAAIGGTANV AEQTSAMQEF
AATLRARGAV EASEIGALPT ELATTDLPDQ IDGQPVIGVS DDVLGPKGFE PIGTFVIAGP
PRSGKSTALR ALVTSVRRFD PAVELFHFGG RRAVLREFAP WRRSATTIDD ARALAKELAG
IVGDESIPGR IMIVVENVTE FGDTDAERPL KELFQAINRS DHFLVGDGDV SQLSSGYGLV
GELKAGRRGI ALRPETYDGD SLFKVPFPKV ARHEYPEGRG IFVENGAFVT VQLPLVGEGP
IGG
//
