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Database: UniProt
Entry: H8GYN4_DEIGI
LinkDB: H8GYN4_DEIGI
Original site: H8GYN4_DEIGI 
ID   H8GYN4_DEIGI            Unreviewed;       451 AA.
AC   H8GYN4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:AFD26081.1};
GN   Name=ftsI {ECO:0000313|EMBL:AFD26081.1};
GN   OrderedLocusNames=DGo_CA2154 {ECO:0000313|EMBL:AFD26081.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26081.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD26081.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA   Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT   Deinococcus gobiensis: insights into the extreme environmental
RT   adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
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DR   EMBL; CP002191; AFD26081.1; -; Genomic_DNA.
DR   RefSeq; WP_014685564.1; NC_017790.1.
DR   AlphaFoldDB; H8GYN4; -.
DR   STRING; 745776.DGo_CA2154; -.
DR   KEGG; dgo:DGo_CA2154; -.
DR   PATRIC; fig|745776.4.peg.2211; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_2_0; -.
DR   OrthoDB; 9770103at2; -.
DR   Proteomes; UP000007575; Chromosome.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.330; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transferase {ECO:0000313|EMBL:AFD26081.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          131..428
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   451 AA;  48357 MW;  86C364166BD37C0A CRC64;
     MEVKIRNRSR MMQLLALFMF ASLVWAYAQL EWGMPQGAGR TSPTPRGAIL AADGSVLART
     VGKNRIYPQG TLAGQIIGMM GDSSGLEGLE AAYNRDLESG QALKLTIDPR TQANAEAALA
     EGVKSHQGEY GSVVVIETRT GRVLAAASYP PFDPNSWRDY SAETRRNRPF LDVFEPGSTV
     KGLVVAAALN ENLTTPSTVY DTPMRRHVGG RWGSTIGDAV QHPATLTTKQ VLRYSSNVGM
     SHIVEHFPAE KLRNYLTNYG FGQDVQLPTV SAATGRLQPL RKWDDLVRAT NAFGQGMSST
     TLQLAAAYNT LANDGMYLSP RLVEGAGVGE RREVIGPGTA REIRSLLESV VSEGIKHQAG
     IEGYALAGKT GTAQVVVDGK YSATVYDSTF AGFFPADAPR VTVAVMVHGA KVNYHGSMLA
     APIYKQIASG LISEWGTAPK LEAPKPEPAT P
//
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