ID C0BRX8_9BIFI Unreviewed; 1308 AA.
AC C0BRX8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Type VII secretion protein EccCb {ECO:0000313|EMBL:EEG71422.1};
GN Name=eccCb {ECO:0000313|EMBL:EEG71422.1};
GN ORFNames=BIFPSEUDO_03392 {ECO:0000313|EMBL:EEG71422.1};
OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=547043 {ECO:0000313|EMBL:EEG71422.1, ECO:0000313|Proteomes:UP000003875};
RN [1] {ECO:0000313|EMBL:EEG71422.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71422.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM 20438).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG71422.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71422.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) 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:EEG71422.1}.
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DR EMBL; ABXX02000002; EEG71422.1; -; Genomic_DNA.
DR KEGG; bpsc:BBPC_1421; -.
DR PATRIC; fig|547043.19.peg.1479; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000003875; 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; 3.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..677
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 794..985
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1089..1272
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 813..820
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1106..1113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1308 AA; 143346 MW; C21753A8B8D9A689 CRC64;
MAITAEQQNS RLEGPKPPKG KIVLQAPPEL EPSDGVNTLL TSLVPLLGTA SAMVMMLMTN
SGLTGMLTGG MFMVSSLGFV AVNGFRQRSQ RMANLAAARR EYLTYLAGIR KTVRTAGRKQ
RNAALWNAPS PSSLTAIAQE PERCWERVPA DDDFMILRCG THSVPLCLQL ESPELPPLAQ
LDPVSASAAH RFMLAHKTLH NMPYGIDLRK YKRVELLGNE SQTQALARAM ICQAAVWHPA
ECCRVLVLAS ADRMGQWEWV RLLPHNRVLN EKYLEGTYNG HGFMLTSNVR EVDALIGEEV
LNRNRRTGDN EIAPHVLVIN DGFDRTVLSR ESRLFAEDGL GGVTVFDMPN DWGELEEDDV
LRVLYSQTVV EEGLNVLEKR DINMVEVFST ALKPVEIQPD ELTVEEALCI AKRLKSVHVN
ETGDDSSQSV NRKKSPELPD LLGISDIRHI DLAKLWAYRV GKERLRVPIG LFDDTSTAFL
DIKEMGQHGM GPHGVLVGAT GSGKSEVLRT LVLSLALSHS PDQLNFVLID FKGGATFAGM
DGMPHISSII TNLGKEASLV DRMEDALDGE VNRRQELLRD AGNLANITEY EEMRVNGGRS
DLKPLPSLLV VVDEFSELLK AKPEIVQSFV RIGAVGRSLG IHLLIASQRL EQGKLRGLDE
HLSYRIGLKT FSATESRAVL GITDAYDLPS LSGIGYLKSP DGTITRFRAS YVSGVPKGLD
GETTTFQYAV EQMRGKGNPA HVVWLPPLVT PNSLDDFMPD LTVTKEYGLI SPRWRNAGAL
VVPCALEDKP REQRRDVMAL NLAGAGGHVA VVGGPLSGKS MMLRSIVASL ALTHSPLEVQ
FYVIDCGGGA FSSMDGLEHV SGIAAGNEDE KVRRTLAEVS GIIDARERFF KEQRIDGMDA
YRRRRAEGKV DDGYGDVFLV IDGWGVFRGD YDELETKVQQ IVARGLTFGV HVLFSANRWM
EIRANISDLI GTKLELRLGD PSDSQIDRHV ADTVPKGAPG RGLSANKLHT LAALPRIDGG
HDAATVSDGI NDLIAKVRSA WQGHPHGPKL RLLPENLPYE AMMASVMRQK ASNQLAKGNM
VVGIDENALS PVVFDFNTEP HCYLFGDAGS GKSTFLRVII NEIVRSYPDG KAKIFMLDYR
RANLAQIPQS HFGAYLTNDE QATESLDALA EFLKTRIPGQ DVTAEQLRDR SWWTGSEVYV
LVDDYDLVST SRGNPLRALV PYLAQASDLG LHVVVARRTG GASRAMYDPV LQTFHDLGMT
GILLSGDSNE GQLIGKVKPK KAAPGRAQIV TRDQGLFVAQ LSNAVLRE
//
