ID M3C003_STRMB Unreviewed; 634 AA.
AC M3C003;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative cell wall biosynthesis protein {ECO:0000313|EMBL:EME97276.1};
GN ORFNames=H340_27292 {ECO:0000313|EMBL:EME97276.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME97276.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EME97276.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME97276.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
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:EME97276.1}.
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DR EMBL; AORZ01000131; EME97276.1; -; Genomic_DNA.
DR RefSeq; WP_004952648.1; NZ_CP072827.1.
DR AlphaFoldDB; M3C003; -.
DR STRING; 1223523.H340_27292; -.
DR PATRIC; fig|1223523.3.peg.5546; -.
DR eggNOG; COG0768; Bacteria.
DR Proteomes; UP000011740; 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, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..253
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 297..611
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 67130 MW; CC5F12173B3B8BFD CRC64;
MTAPRQQPRR PVPGPARPAA RPARPRVGSR PLRLGSPRPR LRLIGLGLTL VLLVFTVRLL
QVQAVDADAY AARANVNRYI PVTLAAERGA ITDRNGVDLA TTVDAYDITA APDLLTPERT
GLRDAAHKAA RLLAPVLGGP VDEVEEKLTA NPASKYVVLA RQQPPQVWDR IRELKQGKAA
RVRGKHGALN LLTGVNREAH SKRVYPNGDL AAGILGFVNA DGKGGGGLEA QLNTALAGKD
GKRVYAQSGG RQVPTGDLKE QAAVPGSDVE LTIDRDIQWA AQSAIAAQVR ASAADRGYVV
VQDSRSGEIL AMANAPGYNP NDLAHADRAA LGNAALQDAY EPGSVNKVMT MAAVLEEGVA
TPGTRVEVPN RLPRADRAFA DDIDHATWHL TLNGVLAKSS NIGTILASEQ LGKTPEESGA
VLYSYLRKFG LGQPTGLGFP GETPGILAPA REWSASQRYT VPFGQGLSLN AVQAASVYST
IAGGGERVRP TLVRGTKGPD GRYIPAPAPP RTRVVSEKTA KQLSEMLESV VDDRDGTGTK
AKIPGYRVAG KTGTSNRVDP RTGRYHGYTA SFAGFAPADQ PRVTVYCAIQ NPTRGSYFGG
QICGPVFQQV MSFALKTLQV PPSGSGPPRL PVEY
//
