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Database: UniProt
Entry: ECCC5_MYCMM
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Original site: ECCC5_MYCMM 
ID   ECCC5_MYCMM             Reviewed;        1388 AA.
AC   B2HST4;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=ESX-5 secretion system protein EccC5 {ECO:0000305};
DE   AltName: Full=ESX conserved component C5 {ECO:0000305};
DE   AltName: Full=Type VII secretion system protein EccC5 {ECO:0000305};
DE            Short=T7SS protein EccC5 {ECO:0000305};
GN   Name=eccC5 {ECO:0000303|PubMed:22925462};
GN   OrderedLocusNames=MMAR_2665 {ECO:0000312|EMBL:ACC41108.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=19602152; DOI=10.1111/j.1365-2958.2009.06783.x;
RA   Abdallah A.M., Verboom T., Weerdenburg E.M., Gey van Pittius N.C.,
RA   Mahasha P.W., Jimenez C., Parra M., Cadieux N., Brennan M.J.,
RA   Appelmelk B.J., Bitter W.;
RT   "PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the
RT   type VII secretion system ESX-5.";
RL   Mol. Microbiol. 73:329-340(2009).
RN   [3]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA   Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA   Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT   "Composition of the type VII secretion system membrane complex.";
RL   Mol. Microbiol. 86:472-484(2012).
CC   -!- FUNCTION: Part of the ESX-5 specialized secretion system, which is
CC       responsible for the secretion of EsxN and a number of PE_PGRS and PPE
CC       proteins (PubMed:19602152, PubMed:22925462). This component is
CC       essential for ESX-5 complex stability and secretion (PubMed:22925462).
CC       {ECO:0000269|PubMed:19602152, ECO:0000269|PubMed:22925462}.
CC   -!- SUBUNIT: Part of the ESX-5 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components. The ESX-5 membrane
CC       complex is composed of EccB5, EccC5, EccD5 and EccE5.
CC       {ECO:0000269|PubMed:22925462}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22925462}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutant does not secrete EsxN and PE_PGRS
CC       proteins, and has reduced levels of EccB5, EccD5 and EccE5.
CC       {ECO:0000269|PubMed:22925462}.
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DR   EMBL; CP000854; ACC41108.1; -; Genomic_DNA.
DR   RefSeq; WP_012394382.1; NC_010612.1.
DR   AlphaFoldDB; B2HST4; -.
DR   SMR; B2HST4; -.
DR   STRING; 216594.MMAR_2665; -.
DR   KEGG; mmi:MMAR_2665; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_003134_1_0_11; -.
DR   OMA; QPSAQVW; -.
DR   OrthoDB; 9807790at2; -.
DR   PHI-base; PHI:6277; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF1; ESX SECRETION SYSTEM PROTEIN YUKB; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1388
FT                   /note="ESX-5 secretion system protein EccC5"
FT                   /id="PRO_0000434750"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          477..679
FT                   /note="FtsK 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   DOMAIN          855..1049
FT                   /note="FtsK 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   DOMAIN          1158..1351
FT                   /note="FtsK 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         500..507
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         873..880
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         1175..1182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1388 AA;  152570 MW;  1BFC4383FBB63A31 CRC64;
     MKRGFARPTP EKAPVIKPEN IVLPTPLSIP PPEGKPWWLI VVGVVVVGLL GGMVAMVFAS
     GSHVFGGVGS IFPIFMMVGI MMMMFRSVGA GGQQQMSRPK LDAMRAQFML MLDMLRETAQ
     ESADSMDSNY RWFHPAPSTL AAAVGSPRMW ERKPDGKDLN FGVVRVGVGM TRPEVTWGEP
     QNMPTDIELE PVTGKALQEF GRYQSVVYNL PKMISLLVEP WYALVGEREQ ALGLMRAIIC
     QLTFSHGPDH VQFIVVSSDL AEWEWVKWLP HFGDSRRYDA AGNARMVYSS VREFAAEQGE
     LFAGRGSFTP RHASSSAQTP TPHTVIICDV DDPQWEYVIS AEGVDGVTFF DLTGSPMWTN
     VPERKLEFDK TGVIEALPRD RDTWMVIDDN AWFFALTDHV SIAEAEEFGQ KLAQWRLAEA
     YEEIGQRVAH IGARDILAYY GIDDPGNIDF DYLWGSRTDS MGRSRLRAPF GNRSDNGELL
     FLDMKSLDEG GDGPHGVMSG TTGSGKSTLV RTVIESLMLG HPPEELQFVL ADLKGGSAVK
     PFAGVPHVSR IITDLEEDQA LMERFLDALW GEIARRKAIC DSAGVDDAKE YNSVRGRMRA
     RGQDMAPLPM LVVVIDEFYE WFRIMPTAVD VLDSIGRQGR AYWIHLMMAS QTIESRAEKL
     MENMGYRLVL KARTAGAAQA AGVPNAVNLP AQAGLGYFRK SLEDIIRFQA EFLWRDYFQP
     GITVDGEEAP VLVHSIDYIR PQLFTNSFTP LEVTVGGPEI DKVVAHANGE VVEEVEAEAE
     EEGIRVPKVG TVIIDQLRRI NFEPYRLWQP PLTQPVAIDD LVNRFLGHPW QKEYGSARNL
     VFPIGVIDRP FKHDQPPWTV DTSGPGSNVL ILGAGGSGKT TALQTLISSA ALTHTPDQVQ
     FYCLAYSSTA LTTVSKLPHV GEVAGPTDPY GVRRTVAELL ALVRERKRSF LEYGIASMEM
     FRRRKFGGEA GPVPNDGFGD VYLVIDNYRA LAEENEVLIE QVNLIINQGP SFGVHVVVTA
     DRESELRPPV RSGFGSRVEL RLAAVEDAKL VRSRFAKDVP VKPGRGMVAV NYVRLDSDPQ
     AGLHTLVARP AMGSTPTNVF ECDSVVAAVS RLTTSQAPPV RRLPASFGVD QVRQLAARDT
     RQGVGVGGIA WAISELDLQP VYLNFAENSH LMVTGRRECG RTTTLATIMS EIGRLYAPGA
     TSVPAPPPGQ PSAQVWLIDP RRQLLTALGS NYVERFAYNL DGVQAMMGEL AAVLAGREPP
     PGLSAEELLS RSWWSGPEIF LIVDDIQQLP PGFDSPLHKA APWVNRAADV GLHVIVTRSF
     GGWSSAGSDP MLRALHQANA PLLVMDADPD EGFIRGKMKG GPLPRGRGLL MAEDTGVFVQ
     VALTEVRK
//
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