ID D9T686_MICAI Unreviewed; 737 AA.
AC D9T686;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ADL47991.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ADL47991.1};
GN OrderedLocusNames=Micau_4478 {ECO:0000313|EMBL:ADL47991.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47991.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL47991.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP002162; ADL47991.1; -; Genomic_DNA.
DR RefSeq; WP_013287607.1; NC_014391.1.
DR AlphaFoldDB; D9T686; -.
DR STRING; 644283.Micau_4478; -.
DR KEGG; mau:Micau_4478; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_5_11; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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 Glycosyltransferase {ECO:0000313|EMBL:ADL47991.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Transferase {ECO:0000313|EMBL:ADL47991.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 205..350
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 403..712
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 78108 MW; BACE4C21653FF1B7 CRC64;
MPPRSDDPRR DATGSRRGSS RGSEPREPGL GGISDARAYT PRGRTVREGG GAEQRRTPRS
NRSGDPFRPA LQVLDGGRAG RAGTREPATD GARSGRRSTA AGGRAGVVRT VSSRPVREPF
DDDDEDAPPR RRSQPRRPAA QPRRPVRKPR RPPRLGDPRR RLRLGTVLAL ALFASIGVRL
VYLQTVDTPA YADGGLPNRL AVVELPAPRG AILDRGGEPL AHSVEARYVF ADPTRVKDRF
ATARLLSPLL GVPVSDLAEK MHKRTLPGTD TPLQFVYLAR GVEIGTAKRI MELDLAGINV
HRDERREVPG GDLAANLIGF VSQDMNGLEG LEAKYDDVLR GQAGKRTYEV GLGDLAAPIP
GGYSRTTQPQ PGSSLKLTVD RDLQFMTQRI LAKQTAKVKG SVGAAVIIEV PSGEVLAQAS
QPTYDAANPT KVGSPADRDD AATTFVVDPG SIHKAITYGA ALQEGVITPD TAFPVADTIV
RGGVTFRDTH PVGGRTMSIP GMLAFSSNVG TIEIAEKLGK DRLFDYQKRF GLGQATGEGM
PGEAAGRLLP PDQWSGSAYG SVPIGHSVDA TPLQMAAAYA TIANNGTYVQ PHLVKETIGA
DGERSPAAAP TTRSVLSPAN AAALRRMMEA VTTVDGPDGR ATGLAAAVPG YRVAGKTGTG
LRYDGGKQQP GEVGSFIGMA PAENPRYVVA VFVWSPGGGG GAVAAPAFRE MMGFTLRHYR
VPPSLTNKSP KFEVFPR
//
