ID L0DNZ8_SINAD Unreviewed; 575 AA.
AC L0DNZ8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Type II secretory pathway, ATPase PulE/Tfp pilus assembly pathway, ATPase PilB {ECO:0000313|EMBL:AGA30578.1};
GN OrderedLocusNames=Sinac_6502 {ECO:0000313|EMBL:AGA30578.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA30578.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA30578.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; CP003364; AGA30578.1; -; Genomic_DNA.
DR RefSeq; WP_015249661.1; NZ_JH621479.1.
DR AlphaFoldDB; L0DNZ8; -.
DR STRING; 886293.Sinac_6502; -.
DR KEGG; saci:Sinac_6502; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_6_0; -.
DR OrthoDB; 263158at2; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798}.
FT DOMAIN 394..408
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
FT REGION 164..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63952 MW; 4C468BC8DFD64ACE CRC64;
MNSAAPVAGH SLTIQLLLDR EIIDQKKLRE FRARVGELTV HELIKSGLAT DQQIAQTYSE
HLVLPLVTEE TQGGAPSPEM ARLLPEKLCR DQLVVPLSVR GEQLDLAIVT PDAMLVIDEI
QLLTGLRVRP RIAALSIAEV WLDRLFNETH ATEGFIPGTE EFEQIDSDQS EEEDDDDTIL
HLDQPPPPGR NGRVIRMVNQ ILDQAIRSGA SDIHLEPFED TCRIRLRIDG RLQEMPPMPR
STFTMVLSRF KILAKMDIAE KRIPQDGAIG LKSGERRIDL RVSTVPAIVG EKMVMRLLDK
GNIPLDLTTL GLDVRQASDL IESIHLPHGL MLVTGPTGSG KSTTLYACLN LLNESHTNIC
TVEDPVEYKF RGMNQIQVKS QIGLSFATAL RSFLRQDPDI IMVGEVRDQE TAEICLRAAL
TGHFVLSTLH TNDALAAVNR LQDMGIEPFL LASTLRVLEA QRLVRRLCPE CKEPYACEKE
LALRHGLEPG ETLYRPRGCS KCRESGYKGR VGVFEVIRIT PEMARLIQRR TPLPELRAAA
RDQGMKLLID SAVDKARQGV TSLENALSVA IGDQD
//