ID A0A068QPN0_9GAMM Unreviewed; 4732 AA.
AC A0A068QPN0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative RTX toxin RtxA {ECO:0000313|EMBL:CDG17012.1};
GN ORFNames=XDD1_1313 {ECO:0000313|EMBL:CDG17012.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG17012.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG17012.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytosol
CC {ECO:0000256|ARBA:ARBA00023586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FO704550; CDG17012.1; -; Genomic_DNA.
DR RefSeq; WP_045969600.1; NZ_VNHN01000008.1.
DR STRING; 351671.XDD1_1313; -.
DR KEGG; xdo:XDD1_1313; -.
DR HOGENOM; CLU_000137_1_0_6; -.
DR OrthoDB; 9798884at2; -.
DR Proteomes; UP000032721; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd20494; C58_RtxA; 1.
DR CDD; cd20501; C80_RtxA-like; 1.
DR CDD; cd16840; toxin_MLD; 1.
DR Gene3D; 1.20.58.1190; -; 1.
DR Gene3D; 2.160.20.160; -; 1.
DR Gene3D; 3.40.50.11050; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR020974; CPD_dom.
DR InterPro; IPR038383; CPD_dom_sf.
DR InterPro; IPR020972; Dermonecrotic/RTX_toxin_MLD.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR006473; Peptidase_C58_Yopt.
DR InterPro; IPR049824; RtxA-like_C80.
DR InterPro; IPR048568; RtxA_C.
DR InterPro; IPR011509; RtxA_toxin.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF012221; MARTX_Nterm; 2.
DR PANTHER; PTHR12277; ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12277:SF205; ALPHA_BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR Pfam; PF11647; MLD; 1.
DR Pfam; PF03543; Peptidase_C58; 1.
DR Pfam; PF11713; Peptidase_C80; 1.
DR Pfam; PF07634; RtxA; 37.
DR Pfam; PF21735; RtxA_C; 7.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF158842; PMT central region-like; 1.
DR PROSITE; PS51771; CGT_MARTX_CPD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 3648..3833
FT /note="Peptidase C80"
FT /evidence="ECO:0000259|PROSITE:PS51771"
FT REGION 1728..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2972..2995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4275..4309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1578..1612
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1734..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4732 AA; 509316 MW; E461815DD5F73664 CRC64;
MGKSVGRSLA YTFTGVYEDD DDGNNITAIG FGGVINAYGG NDYIVVGSLA ARVNTTWGHD
TIVGGAGYLD IHDTGGDLTV KGGSGYTSIN KTQSGPITYE GISGAVKINH TGDKSGIFYS
GAAGYNSLTR KGLQGDISFK GAGAYNELWH ETNQGNLSFA GAGAGNKIDR TWFNNYQGSQ
GNVTFDGAGA ANVISSRVET GNIHFTSAGA YNHINRKGKA GDITLGGAGA YNRVERTRQV
NDVYSETRGD IRFDGVGGYN SLYSDVAHGD IHFTGAGGYN EITRKGAGND FGSEGIEYAK
AEEVVLTHAT MSGEWIGASH QVTGFKSARE PNTYLFAFED GTHTKINKVK LSNDPATGKL
RYYSTAWYKV GKHLKGLDKQ DISAGGGFQA VNADGAYTLS NLTVEQRKAV SIDAVEQKLT
ENQWVNYGGG VLINAADITL SDAKMGGYAV YGDGTKVDVT AVKSNRMPNT YIYAKAFGRY
KKVVVVELRN DPKTGVLQYF ARPCYKFSER SPDFANETFS ADNGYNPMGT GSYSLSDLHY
RVNTERTISA RVSDMHEYQD LELFKSATDS GESSGDIHFI GAGAGNVIKS NVTRGNVTFN
GAGIANVILH QAQYGDLDVN TGGAANVLVR VGDGRYLAHL LAVGNISIHK GNGNSRIAMG
GGFNTHTQIG DGDAFWSGIG GANVLTQKGN GKVSSILAGG ANILTKMGEG DLESAMFGGA
NIITHISNHD AADAGTSKTS AVTLGGVNVL TKKGKGDVQA VMGGGANVLT HIGEGKTTGI
MLGGANILTK VGDGDTTGIM FGLGNILTHV GNGQTLGVMA GAGNLFTKVK DGTAIAAMIG
AGNIFTHVGN GNDWALMGGA GNIFTKVGDG DALALMLALG NVFTQVGDGM SVALMIAKGN
IATKVGDGDA LSAMIGKGNV FTQIGHGSTF AAMIGGANVL TKVGTGLTAA LMVGKANIYT
HVIRDDKAST SIGLFAGTAN VMTKVGNGTT LAAMFGKANV MTHVGNGLTG VLALGKANIV
TKVGDDFMGV VAASEANVVT HVGDGTTAAV LAGKGNILTK VGDGTTVGLL ISKIGNIMTH
VGNGTTVGFA KGDANIITKV GDGLAIHAAW GKANVLTHAG DGDRDSFAKG DANIITKVGD
GQEVTVVQGQ ANIVTHVGDG DDYTGAWGKA NVITKVGDGR NVVLAKGDAN IVTQIGDGDS
FNALWSQGNV VTKVGDGIQV TAAKGKGNIT TTVGDGLSVT AAHGDLNINT KVGDGVSVNV
AWGKLNVNTK VGDGLNVSVM KGEGNANIHV GDGLNIHASY ARNNVAIQVG NGDFYSLAVA
KSNTQSDKLG TLFSNIKQTL LGVAGSQGIN YLVNGDDANT SGTHKGRGAI DLPAVSSLNG
FKLTEIGEVT SDLQNSLQGA VTGVESPDLG RIEKTLGNEN HLNPNQSRNL IVNGDFEQGT
AGWQHTNGIE ASHSAKAYGL SVEGHGERVS ELDVNGNTHL YQDIQNLTAG EEIVVKFDFA
RRVGSSADNG LEVWWNGEVV FAAANGNTEW QNKALTLTAK AGSNRLEFSG IGLNDGLGYV
LDNVIVTSER SDSGVADYVQ QDQAAQNALQ DKEQAEADRE RLAQERDKQL DAISGTQAQL
EATDLAALNA NGQTQRDAIQ GEAQAVTDEL LAKAKGLEAL DSHAAYHGKS GQQHRDKFAH
GLLEGVQTKL NKANETARNQ LDNAQTAAAG RLGDIKEAVA KSEAGALNAE QNRQHAEQDS
EDARLQAENR KKAALSDEQR AYQAGRDGES AAQKAEQRGQ HEISAADSKT AQVQHDAKGA
KLDGSYKPQR TGATGSGLSG NTDESHDSEN IEKAEQSKSR INPESTVQAD GGFSEELHYL
DEDLNELGHA KEALNRLQIN AGIRVKKSTL TSGHSELSVN QSVNPPAAVV TEWVRNTPKI
SGLDLSGLQA LGEELIRQDI QQEAVKSSAT ESTAAIRAQK VADVYRWLDS DNDLASEKYI
PVPGFDRVDA DIPDEIRQKM VASIEGYLEY CGEKVPKEQH TSLAKLFVDA TIDYDWDKRV
ELVLRLESYD YSFAPVHGDK SIVSFWSGKN FKSYRKVLDA AQTDGKKVVY DIDVKGNAFA
IDLNKQLQRW SNMLEYTSDI PEQERQALQS AISASTRSNT GFWSSLYATG SRDDVYVIAE
GGLRLGNYFW NVELPVLRQL QREGLVGEIR LLDKPAEAYQ GMSPESIGRR LTEAGVAVKA
RFDSLSFAEQ EKLLALNPTG YQPDTLVDLD IKTSAIDNLL NQALPFYGLR TERNLLVRES
DDDDGFEVRP WPGHQSDEFK TIMVEDPTDS AQIKAVERFI LANYDNYDQL PDELYLAEGR
MVSHEQGRTR ILAEKVEGRW NYLPKTDLMS ANELQEAAYV KGKILGDSYR QVLDALKDYG
NIRQDHQDYS LEAVEKLTHL RHQVEGYLLG HPDSARTPAL KNLLSQLNVR MEESRVLAEP
TLASTGKGSF SDLYNKLGNA NLKETKHLYL DEQGDFVTRG KSNIQIALKA QSAENAVEQI
KAAVSGEYGQ PIADAVFANV QARDLAKDGK GIDVSGLRKV HQAIEQQLSP VSATLFVWKP
SDHSRLGHAA LQIGQGRIQI NAEDAGEFNQ KNYVSWWPKG SKSSDIRRIF NVSSEQYPDL
KLRWRDFSQP AGQNTALESD VGSEEGDKFG MQDGTYKLEK FIEKLQAAKG VDEKFADFSD
NLGITMLENP KFLQSSGIPE YISRPFVQQM EAGGVDVFEL GKAFAETLRT AAKQQYSPEV
IEKRTAHVIR QFAERELSDT QDFKASEADQ GRVFRINLAG LDMAAMQAEW HKISQDPDAR
YQLLTDNCSS IVARVLKAGG ADNVIGHTWR PKWGIWTPTE LFNYAQTLQE AQIETYLHKP
NQVADEALEA LGQSDKKDKA LEKVAIDNDG TPPRDKEPLN PIARFLNGEL YGAREDRRNV
GYGTQIILDE AVTKGTANKI TLQGDAGRLT GYYHHGDQKD QGELHQGESH QGKDNPAKKV
VLFIHGSGSS AEEQASFIQS HYQKQGVDML AVNLRGYGAS DGHPSEKGLY QDARTMFRYL
VNDRGIKPEH IIIHGYSMGG PIAADLARYA EHNGQAVSGL LLDRPMPSMT KAITAHEVPN
PAGLTGALAK SVNGRFSVEK NLQGISKQTP IMLLTDNEGL GEAGEKLRAK LAEAGYQVAG
EQTFYGHEDS SRLMSQYADK IVSTLSVSDP VSDPQPENGR VKTGLVEKAL YTLFDAKSGG
KELDQYSFHF TQGESLLNNL EKLVPEIGNV LLTKGNHVES KEFLEGICFA LSGRYLMEER
VHGVGGGKAY LSWLTDAVKA YNDNVVNKKS DIHSVETALL NQYRRQNIGS AIQDLLSMQY
SQTQNMSNLV DREKANQAYG GKLKANGLTG NRIDRSLSND VAGYESVMEQ LRQVDKTTYM
SFMSEDHAMA VTVHKGENQT VWSFYDPNFG IKSFDNYQAF KGFMDSFHKG MITGYKSKFG
YEYLASQEKD QSFYVNYNTF EDGTITQYDG VWKQAREGEQ PYVLRALKEQ DKTFKLGSNI
TGRVVDYRDD AVTLEVTAKK GEKVLVEVES HNFKQAAHLV QSNIDKVFAN PTVGQLTLKV
SGDISVTDEV KVPLKGDVSK DNAPEGIDRI VNNHDVDSWE RAEVKPQSES EGSDSRFNGQ
IIIQTENDPV AAKAAANLAG KHPDSSVIVQ LDADGRYRVV YGDPAALSGQ LQSGKLRWQI
VGHGREESAQ NHTRISGYSA DELALRLKQF STDFKQIGKP DHISLVGCSL ISDDKRDGFA
RRFISALDEH GIRTTVSARS SEVAVDSIGR KYTKDAREQW VHKLTDNKIV LGWNDAGAVE
SHAERVRRGI SESDIILSRV GQTDVGAKAQ GAIAENTQTF HAPKQHDAVD NHSAAKSSNN
QLSYSGNIQV QAGDGEFTVM NWGTSNVGIK VGTGGFKSLA FGDNNVMVHI GDGDSKHSVD
IAGYRALEGA QLFMGNRNVS FNLGRSNDLI VMLEKSIPTP PLVNPFEGAV RISGVLQEIA
GSFNSPDWLA KQDQQWTLEG AKKYVRDLSG LDLTSSVDYQ TLTDLDSQNE RSSRGLRSDL
ENTLNKKYNQ WLSGKGNTPE MGKMSRADKF RQANEKLAFN FAVGGQGADI QVTTGNWNFM
FGDNIQSILD TNLGSLFGLM TQDYTSTGLA KNPFTFTPTD LPRQIKNKLL GNLASVGADT
TLADIFGVDY TPQGGIVSRS GQPVDGVAIL REMLEIIGEF SGDQLQAFTD PEKLLNSLEA
GLNIGADGVK SFAESHGLKA KAPDESQEGQ VSIGKGEQSA PQTDRPFGLP SLDMPNLFAT
LFDKDKQAKV GSQVTNLKEN LTADLLNIQE KTFDFLHNSG HLQGDGDMNV SLGNYNFNWG
GDGKDLGAYL GDNNNFWGGR GDDTFYSVGT SNIFAGGEGH DTGVLMGREN MMFGGTGNDV
AVLVGRINYA YLGEGDDQAF VFGEGGVISG SKGRDYIVAS GNFNRIHAGE DQDYVVTIGN
NNQVNLGEGN DFAAVFGNHN QIDGSTGNNA IKLMGYHSVI NGGTGNDHLI ADVVSKFSQL
NGGEGDDLLV LGGYQNRFKG GTGVNRFVVS GDVIDNVVED IKQGDKIIFN DNINWQNLWF
QRSGYDLVLL TQRHVKDTSA QGQFEALGSV TFNNYFDGNR ADIITQMGDK DAQGEREYTA
FSANAVDSLV QAMSGFAPKM GDSGFIDSLD NKTKSTIVTA WSDTTNGKAK LV
//
