ID W4AS97_9BACL Unreviewed; 687 AA.
AC W4AS97;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ETT34370.1};
GN ORFNames=C169_18469 {ECO:0000313|EMBL:ETT34370.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT34370.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT34370.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT34370.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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}.
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:ETT34370.1}.
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DR EMBL; ASPT01000032; ETT34370.1; -; Genomic_DNA.
DR AlphaFoldDB; W4AS97; -.
DR PATRIC; fig|1227076.4.peg.3811; -.
DR Proteomes; UP000019053; Unassembled WGS sequence.
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 Transferase {ECO:0000313|EMBL:ETT34370.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..266
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 322..654
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 664..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 76190 MW; 4790AA7100C91590 CRC64;
MGFRPYKNVP DEEETKSRFH GRINIFFFSA FLIFCIIIVR LAILQFVEGP ELASQESGGE
QKHFPLQPIR GSIIDASGEK LAYSTASNSL YITLMKDYSE KTDKGKANQP EAEEMAKRIV
QVFNKYGDPN IEQKTVKNVM DDLDLEYIKQ HGYEPRLIKS DLTKEEIAYF MENRAKFPGI
QIVEENVRHY DPDTVAVQTI GYLKKFKGSK DLKDYQAIDQ SNKDQDNPGL IYTEEEWIGY
DGLERMYQEE LRGKSGYLSI PINPQNMVDG VPTMVAPEKG LNIHTTIHKD IQVATEQAIM
DRLQYLHTNP VSGKLHKDAV TGYAVAMEID TGHVVAMATM PDYDSNVWGS GGKITQDVVD
SSGNGTITIY GSGRSGHGFE SMIFLGSVIK PLTVLIGLNE GLFGPNDTYP DQGYASIGRE
GSETKIRNSS GHRIGPIKPQ QAIQQSSNAF MIDWVGKRLV NKYGGEKGVT VWDKYMEQFG
LGVVTGSGLP KEHKGLKNYT DTKAAGSNLA ALAYASFGQQ GKYTPLQLAQ YTVMLANEGK
RIKPQLVSKI TDQNGKVVKE FGREILNEVH FPKQYWQIIK QGMNTQGIAG FEDFKYDFAR
KTGTSEQSYK GVNLDNGVFI AFAPRDNPKL AVAVVVPEGG FGSQSAAPIA RKIFDAYDEV
YGLDGTPHPK KADEQAEDGS PDESGDN
//