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Database: UniProt
Entry: A0A1B9CSS6_MYCMA
LinkDB: A0A1B9CSS6_MYCMA
Original site: A0A1B9CSS6_MYCMA 
ID   A0A1B9CSS6_MYCMA        Unreviewed;      1389 AA.
AC   A0A1B9CSS6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Type VII secretion protein EccC {ECO:0000313|EMBL:OCB45543.1};
GN   ORFNames=A5677_05255 {ECO:0000313|EMBL:OCB45543.1};
OS   Mycobacterium malmoense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB45543.1, ECO:0000313|Proteomes:UP000092683};
RN   [1] {ECO:0000313|EMBL:OCB45543.1, ECO:0000313|Proteomes:UP000092683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3012 {ECO:0000313|EMBL:OCB45543.1,
RC   ECO:0000313|Proteomes:UP000092683};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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:OCB45543.1}.
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DR   EMBL; MBEE01000232; OCB45543.1; -; Genomic_DNA.
DR   RefSeq; WP_065483547.1; NZ_MBEE01000232.1.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000092683; 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; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          476..678
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          856..1050
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1159..1352
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         499..506
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         874..881
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1176..1183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1389 AA;  152538 MW;  F3C612E230438A1E CRC64;
     MKRGFARPTP EKPPVIKPEN IVLPTPLSIP PPEGKPWWLV VVGVLVVGLL IGMVGMTFAS
     GSHVFGGAGA IFPIFMIGGV AMMMFGGRFG GQQQMSRPKL DSMRAQFMLM LDMLRETAHE
     SADSMDANYR WFHPAPTTLS AAVGSPRMWE RKPDGKDLNF GVVRVGVGMT RPEVTWGEPQ
     NMPTDIELEP VTGKALQEFG RYQSVVYNLP KMISLLVEPW YSLDGEREQV LGLMRAIICQ
     LAFSHGPDHV QMVVVSSDLD EWDWVKWIPH FGDPRRQDAA GNARMVYSSV REFAAEQAEL
     FAGRGSFTPR HASSSAQTPT PHTVIVADVV DPQWEYVISA EGVDGVTFFD LTGSSMWTSV
     PERTLRFDDK GVIEALPRDR DTWMVIDEKP WFFALTDHIS IAEAEEFAQA LARWRLAEAY
     EEIGQRVAHI GARDIMAYYG IDDPGRIDFQ ALWGARTDTM GRSRLRAPFG NRSDNGELLF
     LDMKSLDEGG DGPHGVMSGT TGSGKSTLVR TVIESLMLSH PPEELQFVLA DLKGGSAVKP
     FAGVPHVSRI ITDLEEDQAL MERFLDALWG EIARRKAICD SAGVDDAKEY NSVRLRMQAR
     GQDMAPLPML VVVIDEFYEW FRIMPTAVDV LDSIGRQGRA YWIHLMMASQ TIESRAEKLM
     ENMGYRLVLK ARTAGAAQAA GVPNAVNLPA QAGLGYFRRS LEDIVRFQAE FLWRDYFPRG
     LTDDGEEAPT LVHSIDYVRP QLFTNSFTPL EVSVGGPELT PAALTNGETL EADGAPTEDD
     DVEGIRVPKV GTVIIDQLRK IDFEPYRLWQ PPLNQPVAID ELVDRFLGHP WQEDYGTARD
     LVFPIGIIDR PFKHDQPPWT VDTSGPGANV LILGAGGSGK TTALQTLICS AALTHTPEQV
     QFYCLAYSST ALTTVARLPH VGEVAGPTDP YGVRRTVAEL LALVRQRKST FLEYGIASME
     VFRRRKFGGE PGPVPNDGFG DVYLVVDNYR ALAEENEVLI EQVNLIINQG PSFGVHVVVT
     ADRESELRPP VRSGFGSRVE LRLAAVEDAK LVRSRFAKDV PVKPGRGMVA VNYVRLDSDP
     QAGLHTLVAR PALGTTPDYV FESDSIIDAV SRLTSSQAPP VRRLPARFDL EQLREVAARD
     TRQGVGAGGI AWAISELDLS PVYLNFAENA HLMVTGRREC GRTTTLATIM SEIGRLYAPG
     ASSAPTPPAG QPSAQVWLVD PRRQLLTTLG SEYVEKFAYN LDGVQAMMGE LAAVLAGREP
     PPGLSAEELL SRSWWSGPEI FLIVDDIQQL PAGFDSPLHK AAPWVTRAAD VGLHVIVTRT
     FGGWSSAGSD PMLRALAQAN APLLVMDADP DEGFIRGKMK GGPLPRGRGL LMAEDTGVFV
     QVAATELRK
//
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