ID H6NC07_9BACL Unreviewed; 679 AA.
AC H6NC07;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:AFC28039.1};
GN ORFNames=PM3016_1105 {ECO:0000313|EMBL:AFC28039.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC28039.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC28039.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC28039.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP003235; AFC28039.1; -; Genomic_DNA.
DR RefSeq; WP_014368727.1; NC_016935.1.
DR AlphaFoldDB; H6NC07; -.
DR STRING; 1116391.PM3016_1105; -.
DR KEGG; pmq:PM3016_1105; -.
DR HOGENOM; CLU_009289_1_1_9; -.
DR Proteomes; UP000007523; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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: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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW Transferase {ECO:0000313|EMBL:AFC28039.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..264
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 320..657
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 679 AA; 75324 MW; 9825E8B35A873795 CRC64;
MMTSFRSKEP GKRPWDSRRA RVNVLFFIVF VMFSILVVRL ATLQFVQGDE LKQAETEFTE
SSTPIAPIRG NIFDRNGAPL AYTVSTQSLF FRITEGDLSE RMDEIIALAG ELEKIFANYG
NKNLKPLTAA EIVERMDVGF DINKQETKIN GYSYMPRRIK SDLTAEEIAY LLEHRDELKW
LEVTEESARV YDERNLAVHL IGYLRPFSAA VNVENSYLST YRDKKDEYLG DEYVGYDGLE
FLYQEELRGE NGTKSYPVNA AQKITGPYTL TPPIKGNNLI LSMDREVQQV AEDAVTEHLA
AMKRASGGSV LGQGREAVAG YAVAMEVDTG KVMAMASMPD YDPNIWHGGV SGGEWNEIRC
RYLNGAIRER CADVPEKEIS KHPPSLVPLG STIKPLTVLL GLNEKLFAPY ETYNDTGTYT
YGKDKSRVNN SGFKSYGPIN ASKAIEVSSN TFMAAMIGER LYNRGGSPLD VWDQYMKKFG
LGVRTGSDLP GESPGDIYYY DTVKQASTQA ALVQASFGQQ GRYTALQLAQ YTAMLANKGK
RLKPLFVDRI VTYDNKQVVK EIQPEVLGQE TYPDTYWNVI HQGMLKVSKT GFEGSEADYT
VAAKTGTSQM SVAGKSLENA VFIAYAPAEK PKLAVAVVVP EGGYGAYGAA PIARKIFDAY
NERIGLYGTP KVPAGEEPQ
//
