ID   A0A0T7BM75_9CYAN        Unreviewed;       747 AA.
AC   A0A0T7BM75;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=IJ00_01615 {ECO:0000313|EMBL:AKG20176.1};
OS   Calothrix sp. 336/3.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG20176.1, ECO:0000313|Proteomes:UP000065745};
RN   [1] {ECO:0000313|EMBL:AKG20176.1, ECO:0000313|Proteomes:UP000065745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:AKG20176.1,
RC   ECO:0000313|Proteomes:UP000065745};
RX   PubMed=25614574;
RA   Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA   Battchikova N.;
RT   "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT   cyanobacterium isolated from a finnish lake.";
RL   Genome Announc. 3:0-0(2015).
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};
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DR   EMBL; CP011382; AKG20176.1; -; Genomic_DNA.
DR   RefSeq; WP_035149372.1; NZ_CP011382.1.
DR   AlphaFoldDB; A0A0T7BM75; -.
DR   STRING; 1337936.IJ00_01615; -.
DR   KEGG; calh:IJ00_01615; -.
DR   eggNOG; COG4953; Bacteria.
DR   OrthoDB; 499624at2; -.
DR   Proteomes; UP000065745; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          313..344
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   747 AA;  83515 MW;  1E4376BA3EBB9B64 CRC64;
     MKLVNRLPFF PQLRIRHKSV KIAISVILLC LFVRFIPYLA PLRSADIAQT RLSLEFTDRN
     GLPLGTILTR DQEHTAVVRL KQVSPIFIQA ILAAEDGDFY HHGALDLKAI ARATQDAIYT
     KRITSGASTI TMQLARMLDG SPRNLSGKIQ EIWTSWRLFA GMNRDEILAA YINRLPMGGN
     IYGVEAAART YFSIPAKDLN LAQASLLAAI PNNPTYFNPY QHWQRLKKRQ KYVLRRMIQD
     KYISQEDGKL ASIEKVVFQR QQGIIAAPHF LFWLAKQGES NSETSAPIVT TIDRELQQFT
     EAQLRQILAN LKNNNVHHGA ALVVDNHRGE VLAYVGSPDY FSQENIGKND GVQALRQPGS
     TLKPFLYELA LEKGVIKPNS LLADVPTHYA IPGAKLYSPT DYTKNFLGNV RVRIALANSL
     NVPAVKVLEK VGVHSFLERL KELGFQNLNQ SAEHYGLGLT LGSGEVNLWE LTQAYLTMAN
     QGQKLPLTPI ISSAPTPNPP PPSKTWQLIG DMLSDRHARA TAFGVDSVLN LPFAAAVKTG
     TSSNYRDTWT VGFSKDYTVA TWVGNFNGEP MKQVSGVTGA APLWNRIMLH LHEQQEPEEF
     SPPQGMVQLP ICAETGLKPT DKCSSVVQEY FFKEDVANYH QGQSLVRENL DSSFKLASPQ
     NQDIFLVTPG NIGKDKLQLK LVKTPQEKVE WWLNGSKIDE GTQQAIFWSL HPGKWELIVK
     SGELSHRVNF TVELGNYQPK NRGFSVR
//