ID A0A0A2VYA9_BEABA Unreviewed; 1937 AA.
AC A0A0A2VYA9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Outer-membrane lipoprotein carrier protein {ECO:0000256|ARBA:ARBA00014035};
GN ORFNames=BBAD15_g2860 {ECO:0000313|EMBL:KGQ11372.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11372.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ11372.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11372.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Periplasm
CC {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- SIMILARITY: Belongs to the LolA family.
CC {ECO:0000256|ARBA:ARBA00007615}.
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:KGQ11372.1}.
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DR EMBL; ANFO01000219; KGQ11372.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2VYA9; -.
DR HOGENOM; CLU_001981_7_1_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblFungi.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:EnsemblFungi.
DR GO; GO:0042953; P:lipoprotein transport; IEA:InterPro.
DR GO; GO:0006282; P:regulation of DNA repair; IEA:EnsemblFungi.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18139; HLD_clamp_RarA; 1.
DR CDD; cd00090; HTH_ARSR; 1.
DR CDD; cd16325; LolA; 1.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.30.70.920; -; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 2.50.20.10; Lipoprotein localisation LolA/LolB/LppX; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR HAMAP; MF_00240; LolA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR025199; FtsK_4TM.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
DR InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00547; lolA; 1.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR Pfam; PF13491; FtsK_4TM; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR Pfam; PF13412; HTH_24; 1.
DR Pfam; PF03548; LolA; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR PRINTS; PR00033; HTHASNC.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR SUPFAM; SSF89392; Prokaryotic lipoproteins and lipoprotein localization factors; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS50901; FTSK; 1.
DR PROSITE; PS00519; HTH_ASNC_1; 1.
DR PROSITE; PS50956; HTH_ASNC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..73
FT /note="HTH asnC-type"
FT /evidence="ECO:0000259|PROSITE:PS50956"
FT DOMAIN 965..1178
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 293..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1937 AA; 213196 MW; B53CE337923C16F4 CRC64;
MVDSKKRPGK DLDRIDRNIL NELQKDGRIS NVELSKRVGL SPTPCLERVR RLERQGFIQG
YTALLNPHYL DASLLVFVEI TLNRGAPDVF EQFNAAVQKL EEIQECHLVS GDFDYLLKTR
VPDMSAYRKL LDPSWSQTAW HEPIHNLGGA PGAWFADTLF FIFGVMAYTI PVIIIGGCWF
TWRQRDSEEF IDYFAVSLRL IGVLAMVLTS CGLAAINADD IWYFASGGVL GSLLSTAMMP
LLNSSGGTIA LLCVWAAGLT LFTGWSWVSI AEKLGSAVLT VLTFASNRTR RDNTWQDEDE
YEEEHDEDDA PQASAEKRES RRARILRGAL ARKQRLSQKF ANPNGRKTDA ALFSGKRMDD
AEDDVLFSAR GVEADPNDVL FSGHKATLPE DQEYDPLFSG HSAVEPIAAA AAATTANQSW
AAPVPPVAPM PPVSTPAPAV DAEPSAPAIA WEPAPTTVTP DPVIAPAPDH YTSPHPARAQ
QQVTPETHQS WSEPVVPVAQ PVVEPQPAPE PVEEVKYVRP PMYHFEEVEE KRAREREQLA
AWYQPVNEPK PDPYSYAPVK PATPEPAQPS MPASAPVSAP LSAAEMPVPD VTQTTSGVQQ
AAKAAATAAA FSPVFSIASD APRSQVKEGI GPQLPRPNRV RVPTRRELAS YGIKLPSQRM
AEEQARLAES QQSEDDYGDE SDALQQHELA RQFAAQQQQR YGEEYADESW SEADQAEAEE
AELARQFAAQ QQQRYGEPQP QSNAPFSLDD FDFQSSLKEL VDDTPSEPLF TPSFEPVPPP
AQHSQPAVQP SQYAQAAQHQ PAAPEPKESL IHPFLMRNGD DRPLQKPTTP LPSLDLLTSP
PTEVEPVDTF AMEQMARLVE ARLADYRIKA DVVDYSPGPV ITRFELDLAP GVKAARISNL
SRDLARSLST VAVRVVEVIP GKPYVGLELP NKKRQTVYLR EVLDCAKFRD NSSPLTVVLG
KDIGGEPVVA DLAKMPHLLV AGTTGSGKSV GVNAMIISML YKATPEDVRF IMIDPKMLEL
SVYEGIPHLL TEVVTDMKDA ANALRWSVNE MERRYKLMSA LGVRNLAGYN ERVLEAERMG
RPIPDPFWKP GDSMDATHPM LEKLPYIVVL VDEFADLMMT VGKKVEELIA RLAQKARAAG
IHLVLATQRP SVDVITGLIK ANIPTRIAFT VSSKIDSRTI LDQGGAESLL GMGDMLYSAP
NSTTPIRVHG AFVRDEEVHA VVQDWKARGR PQYITGITDD EGSGDGNGGG MDGDEELDPL
FDQAVAFVVE KRKASISGVQ RQFRIGYNRA ARIVEQMEAQ GIVSPQGHNA GMTATGAWAD
AAGDLQGRLD KVGSFHASFT QKVTDGSGAA VQEGQGDLWV KRPNLFNWHM TQPDESILVS
DGKTLWFYNP FVEQVTATWL KDATSNTPFM LIARNQSSDW KQYNIKQNGD DFVLTPKSSS
GNLKQFTINV GRDGTIHQFS AVEQDDQRSS YTLKAQQNGA VDAGKFTFTP PKGVTVDDQH
NTFQPLAARM RPENLAQYIG QQHLLAAGKP LPRAIEAGHL HSMILWGPPG TGKTTLAEVI
ARYASADVER ISAVTSGVKE IREAIERARQ NRNAGRRTIL FVDEVHRFNK SQQDAFLPHI
EDGTITFIGA TTENPSFELN SALLSRARVY LLKSLTVADI EQVLDQAMSD KERGYGGQNI
VLPDETRKAI AELVNGDARR ALNTLEMMAD MAESDASGNR ILQTQLLTEI AGERSARFDN
KGDRFYDLIS AVHKSIRGSA PDAALYWYAR IISAGGDPLY VARRLLAIAS EDVGNADPRG
MQVAIAAWDC FTRVGPAEGE RAIAQAIVYL ACAPKSNAVY TAFKAAMADA RERPDYDVPV
HLRNAPTKLM KEMGYGQEYR YAHDEPNAYA AGEEYFPPEM AQTRYYQPTS RGLEGKIGEK
LTWLTEQDQK SPTKRYR
//
