ID A0A3T0NAN3_9RHOB Unreviewed; 1284 AA.
AC A0A3T0NAN3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=PEP-utilizing protein {ECO:0000313|EMBL:AZV81081.1};
GN ORFNames=EBB79_24525 {ECO:0000313|EMBL:AZV81081.1};
OS Parasedimentitalea marina.
OG Plasmid pw43d {ECO:0000313|Proteomes:UP000283063}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV81081.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV81081.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV81081.1,
RC ECO:0000313|Proteomes:UP000283063};
RC PLASMID=pw43d {ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP033223; AZV81081.1; -; Genomic_DNA.
DR KEGG; sedi:EBB79_24525; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000283063; Plasmid pw43d.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00158; RHOD; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:AZV81081.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..191
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 223..308
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 1284 AA; 139922 MW; 46AC3767B897B3F7 CRC64;
MLSGVGAIVA TKLGFSPKKG DTAWRYPVRL ITILSMFAVA LLALNYWQYT KQGAAELARL
QATLVRPAQF SGTTIKDATL KEISFSNQEN HPLAISTSEA AALLHNGSTS FYDVRETGEN
AMGTLPGATH IRFPDFLQSQ PVTGDQPVIL FCHNGNRSSE TCEKLAAMGI DCRFISGGIE
KWIVEGNGFS DTEVKSLSDL RAIPDYSNKD ILLGTDDFKS LLDTEDLQIV DTRYPGDFDT
GHLPGAANIP IRALPTDELM RRIDALDPSK PTIAACYDRR SCFMSQVLGL ELAQKGFDFR
GRYTLPWEFF IPPAPKPHIQ DWQAAQQQGL WDKAVSAVAT GLLWVHARSH ILLGLLSLSL
LTRLLVLPVA LKSERDQIIT AETADALKTL KNDLANDPVR RARAVQAFNA DKGLTPMRNL
TALLFLPVMM IGVSAAQMAS SALQIPFLWM SDLGQPDPTY ILPVLFTALA GLYLVWAVAK
TRRQILLWLG LGLPALFAMV FALGAAANAY LCCSLTLLLA QRAYVTGLFT RLRRSVAERA
HKFTLCRLPR GVIPLGMVEE LETSGNKALR LSILKTAGLP VPGGVVIRSD AIADLRQMSE
AQRDIFAAQI WRLAGETPCA VRSSASNEDG ADQSFAGVFD SVLDVTADTM RAALEQVIAS
FTSERAASYD TSAGDENAGN ILVQQMVQAD YAGVMFTQDP TAPGMVMIEW INGCGDDLVS
ARVTPTSLRF GRYTGLPAYA DQDQTLDLAP LLNLGRQIEQ VFGCPQDVEW AYADGQFQIV
QSRDITTLNL GSEQEKARLA EWRGLLDRFG DADPDQPILE QDEMSEVLPR PTPLSFSLMG
RMWSPGGSVD LACRQLGVPY GLPEGPDGHM VNLFGKTYVD VALKLGMTLN VSASKAKQLR
KQARPMIAQF RSDVIPDLAD QLALWQAVDY TALPLRKLIQ AIDTLQQMLV QDIYVEAEKI
NILAGFTMGE ARVAAQNDPA LRNRLMQATL PHAPSSLIAS CKGKKAQTKA LQLMGHRSIF
DYELSSPRYI EAPSLLWSLL DATTDPNPTT PPPANLPGAL SEVLELALAF QDLKEQAKHE
ALRVVAEIRR AVLALGRVTK LDALIFHLTL DEVLSTDWGQ PAARQIAQAR LDQAELRRTS
APTAVSLSLR DCEMLSLGKQ AQASDSSLGG TCVSGDGSVT GRVFWVEDES AIDPALFDGF
RDGDILVCRM INPAWLPWVQ RSGAVLSEVG GWLSHMAIVA REKDILMLVA CKGLDQLEAT
SRVKVSSDGT IEMSQTAELK VVSA
//
