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Database: UniProt
Entry: A0A0Q2QHN1_MYCGO
LinkDB: A0A0Q2QHN1_MYCGO
Original site: A0A0Q2QHN1_MYCGO 
ID   A0A0Q2QHN1_MYCGO        Unreviewed;      1337 AA.
AC   A0A0Q2QHN1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:KQH79365.1};
GN   ORFNames=AO501_14180 {ECO:0000313|EMBL:KQH79365.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH79365.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH79365.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH79365.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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:KQH79365.1}.
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DR   EMBL; LKTM01000112; KQH79365.1; -; Genomic_DNA.
DR   RefSeq; WP_055577914.1; NZ_LKTM01000112.1.
DR   STRING; 1778.A9W97_01810; -.
DR   Proteomes; UP000051677; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR023836; EccCa-like_Actinobacteria.
DR   InterPro; IPR023837; EccCb-like_Actinobacteria.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03924; T7SS_EccC_a; 1.
DR   NCBIfam; TIGR03925; T7SS_EccC_b; 1.
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; 2.
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:UP000051677};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          461..661
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          816..1019
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1119..1303
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         484..491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         835..842
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1136..1143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1337 AA;  145433 MW;  449CFD9ED0600438 CRC64;
     MSTQGFVRRL RVSPPRMPGG EVNLQPPPEV PRVIPGSLLM RLLPFVMIVA VIGMIALMVT
     VGGRDLMKNP MFLIFPMMMV MSMAGMFIGG GGRSGKAAAE LNEERKDYFS YLANLRDDAD
     MTGAGQRTAL EWSHPDPRAL ADVVGTRRMW ERRPTDTDFC HVRVGIGTHR LATRLLAPET
     GPPEDLEPVS TVALRRFVKT HSVVHALPTA VSLRAFPAIT FEGDRKLARQ LVRSMVLELC
     AFHGPDHVQV AVVTANPDGE SWSWVKWLPH AQHATARDGM GSMRLLFPTL ELLERSLATD
     LGERGRFSRN AEPTKGLKHL VVVIDDGYIA GTERLVTDAG LDSVTLLDLN GADAPANRRG
     LQLVVDGDDV GARTAVGVER FATPDTITVA EAEATARRIG RYRLASAAHI VNLEADARAT
     DPGLMALLKI PDAAEIVPEQ VWRKRSPRER LRVPIGYTPN GQPLELDIKE SAESGMGPHG
     LCIGATGSGK SEFLRTLVLS MVTSHSPEVL NMVLVDFKGG ATFLGLEGVP HIAAIITNLE
     DELILVDRMR DALAGELNRR QELLRSAGNF PNVNEYERAR ANGAELDPLP ALFVIVDEFS
     ELLSQKPDFA ELFVMIGRLG RSLHVHLLLA SQRLEEGKLR GLDSHLSYRI GLKTFSAGES
     RSVLGVPDAY HLPSVPGSAF LKCDAAEPVR FNTCYVSGEY VRPRRAQTGR GRQLGALAPK
     LFTATPVKKD ALPAAPAVEP EAPSVSSTPV RTTLLDVVVS RLRGHGRPAH EVWLPPLDES
     PAVNQLLADA DWSAPENLDG RLWLPMGVVD RPYDQRRDVL MVDLSGAQGN VAVVGGPQSG
     KSTALRTLIM SAAATHTPEQ VQFFCLDFGG GTLASLVNLP HVGGVAGRMD ADGIRRTVAE
     VAGVLRAREV RFRDLGIESM RDFRQRKAHL ATLPPEVAAR DPLSQDKFGD LFLVIDGWAS
     IRSDFEILEP TLNSLAVQGL SYGIHLVISA TRWMEMRAAV KDMLGTRIEL KLGDALDSDV
     GRRFNELIPV GRPGRGMSHE RLHILIALPR LDSNSGVEDL PEGVSAAVKA MRAHYGTRQA
     PRVRMLPHKV DRAAVVRVAR SAGRLGRARF AIGINEAELM PVVLDFDVQP HLVVFGEGEC
     GKTGLLRNIA TGLMENATSE QCKIVLVDYR RSMLGVVGND YLGGYATASQ SCTELMTALA
     GTLRERIPPS DITQQQLKER SWWSGPDIFV MIDDYDLVAT GSIGSPLSPL VEFLPQARDI
     GLRIVVARRI GGAGRAMMDP FVGRLKDLSC NALVMSGTKD EGALFGYKAT EMPPGRGMLI
     SRTTKSGVIQ LSRMPDL
//
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