ID A0A1U7MNR7_9MICO Unreviewed; 609 AA.
AC A0A1U7MNR7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Peptidoglycan glycosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BJF81_06215 {ECO:0000313|EMBL:OLT19992.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT19992.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT19992.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT19992.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:OLT19992.1}.
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DR EMBL; MKKA01000059; OLT19992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7MNR7; -.
DR STRING; 1904966.BJF81_06215; -.
DR Proteomes; UP000185694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IPR005311; PBP_dimer.
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; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000185694};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 51..213
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 255..561
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 64790 MW; 661313F6C190099B CRC64;
MGHPRTRTRV LLLAVLLVLS LFGAQLVRLQ GLDAASVSAA ALDGRLNVTA IPAPRGAITD
VDGAGLAVSV ERRKVIADPT LAEDYVLRDD EGEEVARGFA AVAQVVAEVT GEKEADVLRR
LEEPLGEQYA VVAPDESPAT WQELRSRNVR GLSAENVMRR DYPLGEAAAP LVGWIGAGEM
PAGGLELVHD EQLTGTPGEA VFEVGREGER ITTGLYQEDD AEPGQDVRLT LDADLQWYAY
DAVRQRVEEA GALSGYAVIL DARTSRVLAL ASYPTFDPAD DSQTSEGMRN AAVEDVYEPG
STAKVITAAA ALEKGLVQMD TPIEVPVRLQ RGGTTFKDAE EHPLRHLTFA GVLARSSNMG
TILYGEDLED QELYDWFRKF GIGTTRGLGL PGESVGLLPE PGTWSATTRY TVMYGQGVSS
TLLQQATVFQ TIANDGVRVP ASIVAGTTDA EGRYTETSVP SGKRIIQEET AETLTTIMQQ
VASTGGTAPA AAIEGYHVAG KTSTADRYDQ EKGRYEGVTS SFMGFAPADD PRFVVAVAIQ
KPTRIHTFGG VIAGPVFSKI MRYALVKEGV EPATTAPPTV PLEYDPGEPA PDGSGATLGR
IAIRDEGTG
//
