ID A0A0M8WGS6_9ACTN Unreviewed; 1493 AA.
AC A0A0M8WGS6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Nickel transporter {ECO:0008006|Google:ProtNLM};
GN ORFNames=ADL01_09465 {ECO:0000313|EMBL:KOV83907.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV83907.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV83907.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV83907.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV83907.1}.
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DR EMBL; LGDW01000066; KOV83907.1; -; Genomic_DNA.
DR PATRIC; fig|1519490.3.peg.2070; -.
DR Proteomes; UP000037738; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000037738}.
FT DOMAIN 123..176
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1371..1487
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 557..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..308
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 792..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..922
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1004
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1420
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1493 AA; 153838 MW; FF3FF9AD7EDF2371 CRC64;
MVLVNANGTV VNANTIALGA FETPGTALVG RGLLDLLPEF DSRLIPGTMR RPDSMDPYGQ
TKPTRMIARR TDGSEFPVEV TSANLENGQQ AYDSYGYTND ELLMLVVRDL SGTVDTEAEL
ARSQRQTEMI LRAAAEGVVG TDTEGRVVLV NPAAAQILGY RASDLGGREL HTLVLHSRAD
GEPFPYGESP LADTLRSGRK HRVRGQVLWS KSGDKVSVDL TTAPVRDGDQ LVGAVMTFTD
RRPYDSLAEE KDAADRLHQE ELERVAEEHA SELTALRQQH VTEIERLREE HEEELAAGED
RYAALAEREQ DRYEALAGRQ EQLLVLLGRS LRGPLDELRR DLSALAADDA GQLWPEANQV
LHHLSAGYSR ITTLVDNVLS YQRLDTGAES VTRTKVMLDA VVAAGVDGAV ELIGPGRVQF
AVHAPPIEAE VDPQRLAAAL AHLIADVAGV DATGNSPASA GGYMDNTVVV AAAQRGEVVR
IEVRGPYPGG DPVHEPIVRG IVRAHGGVLQ THEVPGMSGS AFVLEVPIGG GAGAVVADAE
DIEDVVETAV GAELALPEQA VDSNGADGGD GNGGVSGRRR ARRSSVDAFL ESDSPEGAAE
AETDVEAGGA GNEAVAPTGR RRRRATEEAA AASGPAPQPS AEGDGGTGRR RGRPSPVEGG
DAGAGDEGGV SEGAVVMAGE HGAGTAAAGT GLGGTVPPQG VPGAPARRAG GEQHALPPAL
PAAPAAGEGA EGAEGEGGQP TGRRRRALAA AAERGVAQEA GPRPVFALPP AEADRTDQGA
PAAPAGPVGD QFDDGGRHDG LTHDHDEDHT PPQPHPTSTP TGRRRARQAP DQPGTVPPGG
IPGQAVPAQA PVPAPAAQAA VGPQGGVPGQ GQPVPAQGMP GQAAPMAQVA QAGQVAQAMP
GQPVPAQGLP AQPMPPSQPM PGQSVPAQGV QAVQGIQGQQ VPQQALQQAM QQAPQAVAPQ
VPAQGTAPQP AQIQGLAPSQ PAPAAQVPPV AQPQPQPWPP ADDETPDMGT PMQPNLNPNT
AAAAPAPAPA PAPAPAPQAA AVLPPERVTP PRLAQALPAE DVAPVDPNSA QGPAISVRTL
GQGVPFARQA AQVQAPGQPQ SATPPNGTNG TNGSGRRRKL GTRPEPAPGQ PETTARPHPQ
AGQAATATPP TAQAAPVPAQ PSLAVQAPLP GQPSLAGQAP LTQAPLPAQP SLAGQTQLAP
GTPRLPGFTE GAGRSYAIGA PDENAAEGPE PLDGPGGAVE VSDQPQPRPM DDELPPEPLD
NPRRLLVWPA PDVTTQQALS DRGYRPVIVH SREEVNAQIA AFPAALFVDP LTGPITRTAL
QSLRQAAVAA EVPVLVTAGL GQATREAAYG ADPAVLLKAL APRDSEQHPP RVLLIEEHAE
IALALTATLE RRGMQVARAA SDADAVTLAS QLRPNLVVMD LLQVRRRRAG IVDWLRANGQ
LNRTPLVVYT AAVDQADLPR LASGETVLFL AERSTSTEVQ DRIVDLLARI GTN
//
