ID Q104Q1_ALIFS Unreviewed; 557 AA. AC Q104Q1; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 29-MAY-2024, entry version 55. DE SubName: Full=PilB {ECO:0000313|EMBL:ABC11887.1}; DE Flags: Fragment; GN Name=pilB {ECO:0000313|EMBL:ABC11887.1}; OS Aliivibrio fischeri (Vibrio fischeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Aliivibrio. OX NCBI_TaxID=668 {ECO:0000313|EMBL:ABC11887.1}; RN [1] {ECO:0000313|EMBL:ABC11887.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR5 {ECO:0000313|EMBL:ABC11887.1}; RA Browne-Silva J.K., Nishiguchi M.K.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABC11887.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR5 {ECO:0000313|EMBL:ABC11887.1}; RX PubMed=18523167; DOI=10.1099/ijs.0.65370-0; RA Browne-Silva J., Nishiguchi M.K.; RT "Gene sequences of the pil operon reveal relationships between symbiotic RT strains of Vibrio fischeri."; RL Int. J. Syst. Evol. Microbiol. 58:1292-1299(2008). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the GSP E family. CC {ECO:0000256|ARBA:ARBA00006611}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ093343; ABC11887.1; -; Genomic_DNA. DR AlphaFoldDB; Q104Q1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. 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}. FT DOMAIN 378..392 FT /note="Bacterial type II secretion system protein E" FT /evidence="ECO:0000259|PROSITE:PS00662" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABC11887.1" SQ SEQUENCE 557 AA; 61619 MW; ADD79B48ABE763B9 CRC64; ASILRQAELI SATQESSIIE LVQAETHTVP SAILAQGIFT PDELVSHLAQ IFGLEVINVT QFDYAATCQK LGLRDLITRY QALPVSHDSC TIRLAVADPS IAQIEDDFRF TSGKQIELVL ADQGQIQAAI RRVYGAGLSA NDKQHKEITQ DELASLVDVS HDEISATEDL SQDDAPVTRF INQILLEAVR KGVSDIHFEP YEDNYRVRFR CDGILVENSR PSAHLSRRLS ARLKIMAKLD IAERRLPQDG RIKLKLNSTT SIDMRVSSLP TLWGEKIVLR LLDSSAANLN IDKLGYSDQQ KALYLEALKR PQGMILMTGP TGSGKTVSLY SGLNILNTTE QNISTAEDPV EINLNGINQV QVNPKIGLTF AHALRSFLRQ DPDIVMVGEI RDLETAEIAV KAAQTGHLVL STLHTNSAAE TVVRLGNMGI ENFNLASSLS LIIAQRLARR LCNLCKQEDH LSDELREEYN ISSSAIIYQA NKEGCNECTH GYSGRIGIYE VMPFTRELSV AILKGATVRQ IEQIAIQQGM DNLKTSGIKR LEDGTTSLQE LNRVLYF //