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Database: UniProt
Entry: D1AYR0_STRM9
LinkDB: D1AYR0_STRM9
Original site: D1AYR0_STRM9 
ID   D1AYR0_STRM9            Unreviewed;       468 AA.
AC   D1AYR0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Phosphotransferase system EIIC {ECO:0000313|EMBL:ACZ01436.1};
GN   OrderedLocusNames=Smon_0971 {ECO:0000313|EMBL:ACZ01436.1};
OS   Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS   9901).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Streptobacillus.
OX   NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01436.1, ECO:0000313|Proteomes:UP000002072};
RN   [1] {ECO:0000313|EMBL:ACZ01436.1, ECO:0000313|Proteomes:UP000002072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC   {ECO:0000313|Proteomes:UP000002072};
RX   PubMed=21304670; DOI=10.4056/sigs.48727;
RA   Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA   Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA   Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA   Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Streptobacillus moniliformis type strain
RT   (9901T).";
RL   Stand. Genomic Sci. 1:300-307(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001779; ACZ01436.1; -; Genomic_DNA.
DR   RefSeq; WP_012858985.1; NC_013515.1.
DR   AlphaFoldDB; D1AYR0; -.
DR   STRING; 519441.Smon_0971; -.
DR   GeneID; 29673239; -.
DR   KEGG; smf:Smon_0971; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_2_0_0; -.
DR   OrthoDB; 92465at2; -.
DR   Proteomes; UP000002072; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-SPECIFIC EIIBC COMPONENT; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002072};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        113..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..84
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          111..468
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   468 AA;  49870 MW;  6D99A674AC5593C2 CRC64;
     MNARKISEEI FNALGGKENI LSNSVCMTRL RVGIKESVDV EAIKKIEGVL GVVEAETIQI
     VLGPGKVNLI GEEFTKLTGI SLGSFGAKDV ADENKKINKS KHNGKIQQFL QKIANVFVPL
     LPGIISAGLI LGLTNVINIT TKGAFVGQWW FAAIKTIGFG MFTYLAIYVG MNTAKEFGGT
     PILGGIIGAL FVGNAAHPLL SKVNDMPLNL PIINKSFTPS IGGLLASLFM GIIVAKIERG
     IRKVMPTILD TFFTPLFTLL ISVFIAIFLI QPLGNYVTKE IFVILDVVYN KFGIAGGYIL
     SAGFLPLVSV GLHQALAPIH VLLNSPEGPT QGINYLLPIL MMAGGGQVGA GLAIYFKTKN
     KKLKTLTRDA LPVGILGIGE PLMYAVTLPL GKPFITACLG AGFGGLLASL FKIGTITQGV
     SGLFGLLIVK PGTWHLYLIA MLGAYIGGFV LTYLFGVDEE RIESIYGK
//
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