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Database: UniProt
Entry: U7LH81_9CORY
LinkDB: U7LH81_9CORY
Original site: U7LH81_9CORY 
ID   U7LH81_9CORY            Unreviewed;       383 AA.
AC   U7LH81;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=SteA-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF12555};
GN   ORFNames=HMPREF1264_00009 {ECO:0000313|EMBL:ERS57104.1};
OS   Corynebacterium sp. KPL1821.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1203560 {ECO:0000313|EMBL:ERS57104.1, ECO:0000313|Proteomes:UP000017152};
RN   [1] {ECO:0000313|EMBL:ERS57104.1, ECO:0000313|Proteomes:UP000017152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPL1821 {ECO:0000313|EMBL:ERS57104.1,
RC   ECO:0000313|Proteomes:UP000017152};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA   Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Corynebacterium sp. KPL1821.";
RL   Submitted (OCT-2013) 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:ERS57104.1}.
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DR   EMBL; AXLZ01000001; ERS57104.1; -; Genomic_DNA.
DR   RefSeq; WP_023021612.1; NZ_KI515751.1.
DR   AlphaFoldDB; U7LH81; -.
DR   PATRIC; fig|1203560.3.peg.8; -.
DR   HOGENOM; CLU_046690_0_0_11; -.
DR   Proteomes; UP000017152; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   InterPro; IPR047795; Put_SteA-like.
DR   InterPro; IPR022215; SteA-like_C.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; NF040608; division_SteA; 1.
DR   Pfam; PF12555; SteA-like_C; 1.
DR   SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          328..380
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  40376 MW;  6A435B306BD2A484 CRC64;
     MALFSRNPEQ PGALRDCTPG AKGMKKFSEG DVAVIDAANI SRHEAQTLVD LKPSAVINVA
     EFSTGTVPNY GPHILLDADI ALVEGVGQSF VSEFKDGKKA RIGEDGTVFS GDKALGTGRV
     VTRERAEKNF TAAQGALIDH MESFFGNSID FINSEGPLLI DGLGVPASGS EIAGRKVVLF
     SPTDRHREQL KQLRNFIREY EPLLIAVGEA ADSLLAQGYK PDFIIGDPNS VSDEALRCGA
     RVVVPADPEG EVEGLDRIHD LGIGAMTFPA ATHSGTDLGL LFADYHGADL IVQAGGGVDL
     DDIFADRTNP SAVLSRLKAG TKVVDADAVI NLYSAPSSNL GWLWALLGIL VAIAAVILIV
     GFGGSQDFAS NLSETWSRLF GGA
//
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