ID A0A0G0LK32_9BACT Unreviewed; 631 AA.
AC A0A0G0LK32;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:KKQ92258.1};
GN ORFNames=UT16_C0009G0003 {ECO:0000313|EMBL:KKQ92258.1};
OS Candidatus Azambacteria bacterium GW2011_GWA2_39_10.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618611 {ECO:0000313|EMBL:KKQ92258.1, ECO:0000313|Proteomes:UP000034706};
RN [1] {ECO:0000313|EMBL:KKQ92258.1, ECO:0000313|Proteomes:UP000034706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KKQ92258.1}.
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DR EMBL; LBVT01000009; KKQ92258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0LK32; -.
DR PATRIC; fig|1618611.3.peg.141; -.
DR Proteomes; UP000034706; 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 Transferase {ECO:0000313|EMBL:KKQ92258.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..252
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 293..618
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 631 AA; 70014 MW; 2BE7CD652A3F8B76 CRC64;
MFKNSYLKKS RSEIEPEEIL LDRKLAMKLE TPLKNNGFLI IFTVSILILG LFWGRAFWLQ
IKNGDYYTSM SNKNSIRFYH SRPPRGIIYD INHQAITSNT PDFSLLIIPA DLPARTDELN
KWISQLAKII KKDNSEIENF IKSLNKNSTE PALFKSNLDR ETLMSLETNS AILPAIFINK
ETRRDYNGGG YFSHIIGYVG KVTGGDLKTD SYYGALDFIG KDGLEAQYEK ELRGSPGKIA
VSVNSENTIL KTLIAKEAAP GNNLILSIDG DLQKFLTNAL NDKIIQTNST GAAAVVLNVK
SGEIIALVSL PSFDFNSQTY GEIIKDKNKP LFNRAIGGFY PAGSTIKPFV ASAALAENII
DPNFKIDDTL GYIKIENQYD PNIVYTYRDW KAHGFVDMRR AIAVSANVYF YIIGGGYKNI
KVLGIDRIKK YLNIFGFGSD LGIDLPGESS GLIPDPAWKK SVKNEGWFTG DTYNVSIGQG
DTIITPLQLA SAIGAVANGG TLWKPKLVLK ITDHRNNSIR EFKPESIRAN IVDESKLKVV
REGLRKAVTE GSAYLLNDLP IKVAGKTGTA QITNTFRKTN AWFTGFAPYD NPEIALAIIV
EGAGEGSTAA VPVAKEVFYW YYNKNYDKMI K
//
