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Database: UniProt
Entry: A0KS93_SHESA
LinkDB: A0KS93_SHESA
Original site: A0KS93_SHESA 
ID   A0KS93_SHESA            Unreviewed;       569 AA.
AC   A0KS93;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Type IV-A pilus assembly ATPase PilB {ECO:0000313|EMBL:ABK46662.1};
GN   OrderedLocusNames=Shewana3_0419 {ECO:0000313|EMBL:ABK46662.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK46662.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) 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; CP000469; ABK46662.1; -; Genomic_DNA.
DR   RefSeq; WP_011715633.1; NC_008577.1.
DR   AlphaFoldDB; A0KS93; -.
DR   STRING; 94122.Shewana3_0419; -.
DR   KEGG; shn:Shewana3_0419; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_1_6; -.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP000002589; 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}.
FT   DOMAIN          387..401
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   569 AA;  62776 MW;  6FC972F1A7B514FC CRC64;
     MPSAGLHLGL STLFIRKGLL NEEQMASAIT KSRQNKQTLV TTLVQTKLVS ARSIAELCYE
     EYGTPLLDLA EFDVSAIPEE FLNKKLIEKH RCLPLFKRGN RLYIATSDPT NIAALEEFQF
     SAGLHAEAIL VEEDKLAKAL EKVLEEDITG LDLSGMDEAA LAGIEVTDTD KRQEENAGEA
     SDDAPIVIYI NKILTDAIRK GASDLHFEPY EKRYRIRFRI DGILHEVSEP PISLAGRLSA
     RLKVMSKLDI AERRVPQDGR IKMKLSRTKS IDFRVSTLPT LWGEKIVMRI LDSSSAQLGI
     EKLGYEPDQE KLYLEMLAKP QGMILVTGPT GSGKTVSLYT GLNILNTAER NISTAEDPVE
     INLEGVNQVH INLKAGLTFA SALRSFLRQD PDVVMVGEIR DLETAEIAIK AAQTGHLVLS
     TLHTNSAAET LTRLINMGVP GYNIASSVNL IIAQRLARRL CTECKQAEQI PEHELQRLGF
     TDEQIAQGFT TFKPVGCEHC SGGYKGRVGI YEVMKMSDEI ARTIMEGGNS LQIADQAKAQ
     GMRDLRQSGL LKVLQGVTSI AEINRVTSF
//
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