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Database: UniProt
Entry: Q4BYI0_CROWT
LinkDB: Q4BYI0_CROWT
Original site: Q4BYI0_CROWT 
ID   Q4BYI0_CROWT            Unreviewed;       771 AA.
AC   Q4BYI0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=CwatDRAFT_1923 {ECO:0000313|EMBL:EAM48954.1};
OS   Crocosphaera watsonii WH 8501.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM48954.1, ECO:0000313|Proteomes:UP000003922};
RN   [1] {ECO:0000313|EMBL:EAM48954.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48954.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   DOE Joint Genome Institute;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAM48954.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48954.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M.;
RT   "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAM48954.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48954.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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:EAM48954.1}.
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DR   EMBL; AADV02000102; EAM48954.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4BYI0; -.
DR   KEGG; cwa:CwatDRAFT_1923; -.
DR   Proteomes; UP000003922; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003922};
KW   Transferase {ECO:0000313|EMBL:EAM48954.1}.
FT   DOMAIN          88..141
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   REGION          752..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  85732 MW;  70E455C9B6031113 CRC64;
     MRRNLLPHFR PTKRGQGLGS QIFHERSAYL NMSQKQPISQ LLTQVVQNLM KSNPKKKVLK
     KGAKVPEIRV KESPKDKLIK YPLIGDRHII GRSSSNTDIK VLNPIVSQVH CSLHRDQKNP
     HHFIIKDENS TNGIYLKKRR VNNLFLRHGD TLTFGPPELN DIATLTYYNP PPKWAQVLKY
     GFYGMGSLIT LGVAWLLWET SKIKVHPLPK GVPGPVVVYA RDRQTPLSTL NDDPHQEVKN
     LKDFSPHLPN ALIASEDTRF YWHIGVDPYG IFRAIVVNLQ DDGISQGAST LTQQVARSLF
     PEVGRENTAQ RKIREMIVAL KLEAVYSKDF LLKTYLNRVY LGVGKYGFED AAQFYFDKSA
     TEVDIAEAAT LVAMLPAPNL YHPVQDYNTS VQLRNRVIDR MAALRMISPE EAARARRSII
     DLSPQARKAL ANNKAPYFYN HVRQELRQLL GTEIAKEGNF IVETGLDLNK QALAEKKLQQ
     AVKTQGKTDG FSNGAMVTLD TRTGEILALV GGVDYKQSQF NRVTQAKRQP GSTFKLFAYA
     AALEKGISPQ KTYSCGGIRW QGQAYKPCER SSGETDMYGA MAQSENTIAL QVAREAGLNS
     VVNVAQRLGV KSKLQAVPGL VLGQSETTVL EMTGAYAAVA NDGVWNRPHA IRRILDGGDC
     TNNNDWRTCR EIYNFQTDNS ARQQALSPQV SRTMTRMLKT VISNGTGRAA SVGLGEAGKT
     GTTDRAVDLW FIGYIPRKNL ATGIWLGNDN NSATKGSSGQ AAALWGSYHR P
//
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