ID   W5TBT6_9NOCA            Unreviewed;      1338 AA.
AC   W5TBT6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Putative type VII secretion system protein EccC {ECO:0000313|EMBL:AHH16413.1};
GN   Name=eccC {ECO:0000313|EMBL:AHH16413.1};
GN   ORFNames=NONO_c16120 {ECO:0000313|EMBL:AHH16413.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH16413.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH16413.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH16413.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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DR   EMBL; CP006850; AHH16413.1; -; Genomic_DNA.
DR   RefSeq; WP_025347923.1; NZ_CP006850.1.
DR   STRING; 1415166.NONO_c16120; -.
DR   KEGG; nno:NONO_c16120; -.
DR   PATRIC; fig|1415166.3.peg.1639; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_003134_1_0_11; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000019150; Chromosome.
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; 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:UP000019150};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          459..659
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          813..1014
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1117..1299
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         482..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         832..839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1134..1141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1338 AA;  145583 MW;  69FD8B91A09109EE CRC64;
     MTTTRRFVRP ARAERGPKAP AVTELRLQPP TELPKPVPPS RIKMIMPVVM VAGMGGMMVM
     MFRNGGASLN PMMMMFPVMM LVSMFGMLGG GMSGNGGGGA ASLNEERKDY LRSIGENRKT
     VHTAETELYE YLRHTHPGPN EIARLVGSKR MWEVQVASPQ FLRVRIGRGR IANQVRVIVP
     EAAPTSDLDP VGVVEVTRFA KAYSTVGGMP VAINLLSAPQ VGLDGDPDMV AALVRSMIAE
     LAVMHGPDQV AVAAVLPDPD APQWSWLKWL PHTQHPSDTD AIGSSRMVYR SVSELRAKVL
     AGLNRGPFSA NSQPTLDRTH YILIVDVGGP ASERDISGVD GCTWIRMGAT EQDLPRALKF
     TVSAERELHE VTPRGPRKVG VADGISMSAM GALARGLSPY RLSTVVEAVV ADQAGTGTSW
     EEMVGIADPG SILVERQWPV RRDIDRNRLN IPFGHDPAGQ IVHLDIKESA EEGMGPHGMC
     IGATGSGKSE FLRTLVLSAV ATHSPDVLNL LLVDFKGGAT FLGFDRLHHV TAVVTNMEEE
     ADLVTRMEDV INGEMARRQR VLRDAGNFAN VADYERAREQ GAQLAPLPTL LIILDEFAEL
     LEQHPNFAKL FVAIGRLGRS LRIHLLLASQ KVPASRMGEL EAHLSYRIAL RTNQTSDSRD
     AIGTADAYHL PKKPGSGYLR VGSGDLQRFQ AAYVGSPYQP PAQVATSADA QRARRPGGGY
     KPPQQFTTAH IVATRTETIV EPQIVVPDSD DDADVASLMD TVLTQIGGHG RQAHKMWLPP
     LGVPPTLERL TPAVQPGMLH VPLAVVDKPR QQRQDVWTVD LSAAGGHVAV VGGPQSGKST
     ALQTLALSAA LTHTPEQVQF YCLDFAGGLT GLRQIPHVGS VASARDTDRI RRTFALVTNL
     IASRQALFAE LGIDSMREFR RRREDPGKSA QLTAHGDTHG DVFFMIDGWD IGFSVNGPYF
     DEYLPVVESI ALQGLNYGIH LVISSSRWTA VRPNIKDLMQ TRLEMRLGDL TDTVFSAHRA
     VVASIPADRP GRCLSTDGLH MLTALPRIDG VGDPENASQG LAAAAAELQR RYGDRRAPEV
     KLLPARITLP EIIAGRPQPE TLAQRLVVPF GVRESDLSPA TIDFGVSTHL AIFGAPGCGK
     STVLAALLQS IRNQFTPDQA KVLLVDYRRQ HMEAIPPEQS IGYLTAERDL IEGLPLLVDK
     LRGRRPPDGV TPQQLRERSW WSGPEVFVVV DDYHMVAPRG QLNPLDPLRD IIVDGRDTGF
     HLITSRNIAQ ADMSLYDNVI GQIKNLNSSG FIMDGSKLDG MLIGDVKPTK QPVGRGIFVE
     PLHSRRDLVQ AAWMPEPE
//