ID   A0A1B8UUV9_9BACL        Unreviewed;      1343 AA.
AC   A0A1B8UUV9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Type VII secretion protein EssC {ECO:0000313|EMBL:OBY80150.1};
GN   ORFNames=BBG47_07705 {ECO:0000313|EMBL:OBY80150.1};
OS   Paenibacillus sp. KS1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY80150.1, ECO:0000313|Proteomes:UP000092663};
RN   [1] {ECO:0000313|EMBL:OBY80150.1, ECO:0000313|Proteomes:UP000092663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS1 {ECO:0000313|EMBL:OBY80150.1,
RC   ECO:0000313|Proteomes:UP000092663};
RA   Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT   "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT   isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT   Florida, USA.";
RL   Submitted (JUN-2016) 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:OBY80150.1}.
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DR   EMBL; MAIS01000016; OBY80150.1; -; Genomic_DNA.
DR   RefSeq; WP_065291249.1; NZ_MAIS01000016.1.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000092663; 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   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; 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; 3.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS50901; FTSK; 3.
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:UP000092663};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          461..658
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          810..992
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1107..1279
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         485..492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         826..833
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1124..1131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1343 AA;  152395 MW;  E4CEB260802F8E90 CRC64;
     MNVMYQRSPR IKPELPEEKL EILRPPAEPS RPTFSIVTLI IPIVMTLVSI GFYIYMSMSG
     KMGNSNYMMF QMITISMMLM SYTLPFFLYL SNKRQYVRKQ AERSQMYLAQ LEKHRLEIIE
     KQHEQRAAMY AIHGDPDVCH QIVKNRNSSL WERGPFDVDF MDVRIGTGEV PFYMPIITPR
     TDGYEKDPLI EAAHKLEQDS RSVDEVPITL PLYESKVVGI VGDRASVMEA VRIVIAQLTT
     RHSPDEVKLA ALYNEQEAEN WGWLRWLPHT WNDDRTQRYL ADRRSTAHQL ADQLYGILNR
     RKSFQTTGEK KKQLPIYVVL LQDSQMIEEE PLYPLLLEEA SRVDSCTLVL SDRKERLPMQ
     CRLIVEVGAD TAVSTQKTDQ EGIVQHSFHM DHLSADKIDT LARYMAPIRL KRSAASDLPP
     VLTLFDMFGV EQVEQLKLVE RWNRNRYPDT LPVPVGVRAG GKLVSLNLHD KIERKGHGPH
     GLLAGTTGSG KSEVIQSLIA SLAAEYHPHD VAFMLIDYKG GGMSNTFEKL PHVVGTITNL
     DESLIERAQV SLRAELIRRQ HILNDAGNMQ HIDEYYKSPL RYQNPLPHLI IIIDEFAQLK
     KEQPEFMDEL ISIAAIGRTL GVHLLLATQK PAGVVDEKIW SNTRFRICLR VQSEGDSRDM
     LKIPNAAWIT HPGRGYFQVG SDEVFEEMQF AWSGAPYLVK CQEGQPLRIE VSEVRLNGKM
     EALLPSDTLL SAYDEQDQLK QLQVFIDAVA EAAWCEGINR LQGPWLAPLP QELGRSELFK
     RTRTLSGVTG DSKGIQPIVG LLDDVMNQRQ EPLGIEMDHE HWAVYGMPGT GKTTFVQTLL
     MSLAEQYEPD VWHGYVVDMG RMLKDYTDLP HVGAVIAGED EDRLKRLFRY LLAKVKERTE
     MLSEAGVKTI ASYRQVTQLS VPNIVVIIDG YLNFRTSYPD ENECLEYLLR EGGSLAISFV
     ITANRVTDIF DKFRSNISNA ISYELADPSD YYFAVGRPAR TPARLQAGRG LIKHNGVPIE
     FQTAYPADGN NDVERVLQLR SQIRLMHNSW QGAAAPLIRS LPERVRLSEL LKLHDDSYEE
     SEIIEAEQLQ CSERLQPVPV GVRTDDLEPY LVNLKEGPHF VVASPMESGK TSFLTSWMLS
     LAYHMSPERL HIYAIDVRYG DNGVASLRDL PHVREIVTEE ERIPGFIQQV YDQVASRSKD
     GGDPILLLVM DDADMLCKQL TDYTVKDQLS AIVRQGRDKG VHLVLAGVPS DFPTFGVDWF
     NDVKASQAGF LFGTIDANDL SFFRIPISES QSSGPSGSKV LPPGQGYFVR RKFTKIKTAI
     PYDEKWTPAA WTTHIDKRWK VRV
//