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Database: UniProt
Entry: Q6XNC3_RHOER
LinkDB: Q6XNC3_RHOER
Original site: Q6XNC3_RHOER 
ID   Q6XNC3_RHOER            Unreviewed;      1259 AA.
AC   Q6XNC3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   28-JUN-2023, entry version 55.
DE   SubName: Full=Putative regulator {ECO:0000313|EMBL:AAP73908.1};
GN   ORFNames=PBD2.023 {ECO:0000313|EMBL:AAP73908.1};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OG   Plasmid pBD2 {ECO:0000313|EMBL:AAP73908.1}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833 {ECO:0000313|EMBL:AAP73908.1};
RN   [1] {ECO:0000313|EMBL:AAP73908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BD2 {ECO:0000313|EMBL:AAP73908.1};
RC   PLASMID=pBD2 {ECO:0000313|EMBL:AAP73908.1};
RX   PubMed=12923100; DOI=10.1128/JB.185.17.5269-5274.2003;
RA   Stecker C., Johann A., Herzberg C., Averhoff B., Gottschalk G.;
RT   "Complete nucleotide sequence and genetic organization of the 210-kilobase
RT   linear plasmid of Rhodococcus erythropolis BD2.";
RL   J. Bacteriol. 185:5269-5274(2003).
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DR   EMBL; AY223810; AAP73908.1; -; Genomic_DNA.
DR   RefSeq; NP_898638.1; NC_005073.1.
DR   RefSeq; WP_011133366.1; NC_005073.1.
DR   AlphaFoldDB; Q6XNC3; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR005158; BTAD.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR34700; POTASSIUM BINDING PROTEIN KBP; 1.
DR   PANTHER; PTHR34700:SF4; POTASSIUM BINDING PROTEIN KBP; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM01043; BTAD; 1.
DR   SMART; SM00257; LysM; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:AAP73908.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..221
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          231..278
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          284..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..329
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..451
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1259 AA;  132930 MW;  2E80107F70B5E474 CRC64;
     MNVAAARLKG LLYLITLLAL AAGIPFALYT FAGNPLAGVT SLTFDAIKEA LTTQDDGTLF
     LSALTIIGWI AWATFAYSII IELAAALRGV KVRRIKGLQF QQHSAAILVS GALLLITAGT
     ATATPAADIL GPNHASPTSI SAPAFFNDAQ TQSPQQSAPS WTKTPAQTPA GTTIVTESGD
     TLWGLAERHL GDGTRYPEIQ SLNQNAIPDE AWIDAGITLT LPAAPEKQLD GAYTVKAGDT
     LWDLAETYLG DGSRYPEIHG ATGPLTTDVI QIGQQLFLTP AATGAEVAPP APSPNSAAET
     PAAESSAPAP EIAPELVPEP APQPAPELVP DVAVSPTAAA PEAPTAAAPE TPEVPVSSAP
     SEVAGEQSPL VVPDVPELQE LVPGGDEMAQ AEARAAEEAA ARIFGIEIPG APAAEAAEPS
     VAEAPATEPA PQPAPPVSVD VPAPSEAPDV APAPAPAIDE NSAPASAPTA PGAPDSTISQ
     SEQFNTPEIA PELTPEPTPE TGAQQATPAD TQAPETLVPL NTTAAQLPEN AAATTALTST
     DNAQDSKTVM GLSALAGIAL LAGVGLFRRR QQNRRRRGER IPMPKESTAL VEQQIREIAD
     PSLLDLLDNA LRDVADICRT NSIPLPALLG VFLHDRSIEL ALLDDIELPA PWQRDRETSA
     WTITADDELD PPLTTVSPYP ALVEIGEIES GSRLLLNLEQ LSHLGIAAPT AEARDIVRAL
     AVFLAFSPLG DNLKLTLVGT GEALARPNTD GSALIEYAPT PDAVLERLAR HTRSDAQALS
     DNGIDDIAQA RIEYTDSAIT NPEIILLSEP LTPAQREIFD GILANAPRVA FAAVTAADDP
     TADWTLTTET DGSAKLRRPG APAFHLTPAR ISEAEFDAIV DVLETADADP IANEASQNDP
     WTAESFDDRI AEATSVDDLL PEPAAAVHVL TSELNFGTAA AEFDDSEALT HPLTFIDSVD
     EGDAAANTPS IAMAIAPAPE SGPSIDEHIW IHILGTPRVT ALNEGSDVGR RPHLTELAAL
     IATHPHPGIR GPQVDEKIWP KQTYANLSFS EQTTKRTARR NTAFTRLRNF LGETANGDLA
     FPKVFDNTGN TPYRLDETVY TDWDIWNNLI RGHPASADDN ELTAAVALVE GAPFTTKKAP
     TRYGWAEELR QNIISELTDA IEELSARHLQ EGETRIALEL AQKGLGVDEY HEGLWRLAII
     ATHGSDDITA TQGLIDTLLT KLAELDVDPN EQTAELLQIL DDFHDTTGER PYRITQRAS
//
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