ID L0GWW0_9GAMM Unreviewed; 571 AA.
AC L0GWW0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Type IV-A pilus assembly ATPase PilB {ECO:0000313|EMBL:AGA89855.1};
GN ORFNames=Thimo_1050 {ECO:0000313|EMBL:AGA89855.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA89855.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA89855.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA89855.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; CP003051; AGA89855.1; -; Genomic_DNA.
DR RefSeq; WP_015280000.1; NC_019940.1.
DR AlphaFoldDB; L0GWW0; -.
DR STRING; 765912.Thimo_1050; -.
DR KEGG; tmb:Thimo_1050; -.
DR PATRIC; fig|765912.4.peg.1015; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_1_6; -.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000010816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0009297; P:pilus assembly; 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; IPR013374; ATPase_typ4_pilus-assembl_PilB.
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 NCBIfam; TIGR02538; type_IV_pilB; 1.
DR PANTHER; PTHR30258:SF1; PROTEIN TRANSPORT PROTEIN HOFB HOMOLOG; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816}.
FT DOMAIN 389..403
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 571 AA; 63470 MW; 591B9750034DEE79 CRC64;
MATTQPSLNP SGLAWRLVRD RLITEDVART AHAEASKRRE PFVHYLVQQQ ILDSRRIAIA
ACHEFGVPLF DISALDLQQA PVNLVDERLI RRHRALPIFR RGNRLFLAVS DPTNDQGVDE
IRFNTGLTIE MVLAEEDKLS AAIDRAIEAQ DTTTMTEIMD AELETLDIAS DDDKSNRDND
LNIDEAPIVR YVNKILIDAI TSGASDVHFE PYEKTFRIRF RQDGLLREVA SPPSNLAARL
VARLKVMSRM NIAERRIPQD GRIKLKLSRN RDIDFRVNTL PTLYGEKVVL RILDSSASTV
DVEDLGMDPE QRDVFLEAID KPYGMVLVTG PTGSGKTVSL YSALNLLNKP EVNISTVEDP
VEIVVPGINQ VNMNPKTGLT FAAALRAFLR QDPDIIMVGE VRDLETAEIA VKAAQTGHMV
LSTLHTNDAP QSLTRLANMG VAPFNIASSI LLIMAQRLVR RLCTHCRKPE EIPRETLLVE
GFTEKEIEEG LTIYGPVGCE RCTKGYKGRT GIFQVMKVSD AISRLILEGG NALQLAEQAK
HEGVADLRRS GLSKVKAGIT SLEELNRVTK E
//
