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Database: UniProt
Entry: B1VH13_CORU7
LinkDB: B1VH13_CORU7
Original site: B1VH13_CORU7 
ID   B1VH13_CORU7            Unreviewed;       396 AA.
AC   B1VH13;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=SteA-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF12555};
GN   OrderedLocusNames=cu1094 {ECO:0000313|EMBL:CAQ05054.1};
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ05054.1, ECO:0000313|Proteomes:UP000001727};
RN   [1] {ECO:0000313|EMBL:CAQ05054.1, ECO:0000313|Proteomes:UP000001727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
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DR   EMBL; AM942444; CAQ05054.1; -; Genomic_DNA.
DR   RefSeq; WP_012360342.1; NC_010545.1.
DR   AlphaFoldDB; B1VH13; -.
DR   STRING; 504474.cu1094; -.
DR   GeneID; 60603872; -.
DR   KEGG; cur:cu1094; -.
DR   eggNOG; COG4825; Bacteria.
DR   HOGENOM; CLU_046690_0_0_11; -.
DR   Proteomes; UP000001727; Chromosome.
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   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:UP000001727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..387
FT                   /note="SteA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12555"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  42448 MW;  E9A5F85DC0A97058 CRC64;
     MVRMMFSRSE KPGITGATRN LTGPKAWSKT KISEGDIVVI SAPDINRATA QRFIDAGVAG
     VVNTAQFTTG QVPNFGPQML LDAGIELVEN VDPEITEKVK NGKKGRLEGG HLYYGDRSLG
     SGAILDLDAS MQRFDDARSA LGDHLDALAG NTAELARSES PLLIDGLGIP DVDVDMVDRK
     VMVISPLPDL KDQLRDLRFF LREYDPIIVA IESAADELLE LGYRPAVIVG NPENIGSESL
     RSGATVVLPA EADGYAQGLE RIQDLGVGAM TFPAATKNPT DLALLLADYH GASMVVHLGE
     KWDLDRVFSE TESEDTPSAL LSRLRVGPKF VDASSIAELY RVSKSGSGWL WALIGVLAAI
     LVIILIAGFS GDAGFVDNLI DSWNNLALSV QGLFKN
//
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