ID A0A1M6C0T5_MALRU Unreviewed; 616 AA.
AC A0A1M6C0T5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SHI54659.1};
GN ORFNames=SAMN02745165_00367 {ECO:0000313|EMBL:SHI54659.1};
OS Malonomonas rubra DSM 5091.
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Geopsychrobacteraceae; Malonomonas.
OX NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHI54659.1, ECO:0000313|Proteomes:UP000184171};
RN [1] {ECO:0000313|EMBL:SHI54659.1, ECO:0000313|Proteomes:UP000184171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5091 {ECO:0000313|EMBL:SHI54659.1,
RC ECO:0000313|Proteomes:UP000184171};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; FQZT01000001; SHI54659.1; -; Genomic_DNA.
DR RefSeq; WP_072905037.1; NZ_FQZT01000001.1.
DR AlphaFoldDB; A0A1M6C0T5; -.
DR STRING; 1122189.SAMN02745165_00367; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000184171; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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 InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184171};
KW Transferase {ECO:0000313|EMBL:SHI54659.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..231
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 263..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 537..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 68809 MW; 5918767913749698 CRC64;
MGLDAKWAEL PSVQRRFLLF TAAVAIIFLL LCLRLWYLQI INYEEFQDRS TRNRTRMLSL
EAPRGPVFDR NGHLLVGNRP SFQISVMRQD VENKDALLLR LSKLLEIDLE VLEKRWQDGR
RYPIYRPVPL AHDVSRELME RVQEHSVELP GVLTEVRPVR DYLEKGSAAH LVGYLGEITD
SELRSEEFEG YQAGDFVGKI ALERSYETYL KGIKGKRLVE VDVKGKLLRQ LQAERALPGN
KVYLTLDREL QRAADEAFGD QSGAAVAIDV KSGDILAMVS RPTFDPALFA RGIASDEWTA
LLNDKRHPLQ NKVVAGQYPP GSTFKMVVAL AAMREGIAGS QRTINCDGDF ELGGMRFRCW
KKAGHGPTDL KKALRESCDV WFYQVGLELG IDKLSAAAKE FGLGAPVGYP LPGEKRGIMP
SREWKRARYN LPWYAGETVN ASIGQGFVLS TPLQLAVMTA ALANGGKVLK PQLIDRIEDW
QGNLLMETGI DIVRQISYSA SAWREIRRGM VAVVNELRGT GQVAKLEQVV VAGKTGTSQV
VRRKSDEEEE EDDNGDVPYR FRPHALFVSY APAEDPQIAV AVVVEHGQHG GSAAGPIAKT
IMERYFADPQ TETEEE
//
