ID M7PA67_9BACL Unreviewed; 911 AA.
AC M7PA67;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=ponA {ECO:0000313|EMBL:EMR07374.1};
GN ORFNames=C772_00390 {ECO:0000313|EMBL:EMR07374.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR07374.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR07374.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR07374.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:EMR07374.1}.
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DR EMBL; AOFT01000002; EMR07374.1; -; Genomic_DNA.
DR RefSeq; WP_008296948.1; NZ_AOFT01000002.1.
DR AlphaFoldDB; M7PA67; -.
DR STRING; 1235279.C772_00390; -.
DR PATRIC; fig|1235279.3.peg.400; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000011919; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 714..804
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..835
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 99436 MW; 8D3E1193223E6571 CRC64;
MSDQIQSRSQ RRKQQEQARK TDRKGSKKPG GKKKQPLWKT ILKIAVIVAV AGFVFGAGLF
TYYAATAPEL DEESLKDPLS SELYVEGSEE PLITLGPEKR EHVEYEQIPQ IMEDAILATE
DVRFYKHHGM DLWRLGGAVL ANFRDGFGAQ GASTISQQVV KNSFLQNEKT LKRKAQEAWL
AFQLERKYEK EEIFEMYFNK VLMTDNIYGF GTAADQFYGK EPEELELHEA ALLAGMPQSP
NRYNPYRHPE RAEKRRNVVL GLMVQHGKIS QEQADAAKAV PVREGLIPPE EQKHHGNNKY
AAFVDMVREE LEEHDLSTAD GLKIYTTLDP AAQEKVESTI SSENIEAKTG KNPLASAAVI
DTKTGAIKAI AGRPDYRSGD KNLALVDDRS VGSTIKPILD YGPAIEYLDW STGQTVDDER
RTYKGSDQVI RNANGRYLGK MTMRKALYMS QNVPAVSTFE EVGPEKAADF AKNVGINIEN
PNSSSALGGG VGASPLQMAS AYASFGNGGM YTKPYTINKV VMRDGKTERD LRPKPASAMK
DSTAYMITDV LREVVKNPQG TAYRHVSSHG LDVAGKTGTT NYDTKTFEER FSGEDMAVPD
SWFVGYTPEY SIAVWTGHQD YYTPLTEWEE RWFPQRAFSE ILGDLAQRGE HSSFKKPKSV
VEATIEVGTD PLRLASDWTP SDRKSTELFV RGTVPERVSK TYEPEEEETE TLPAPTGLSA
DYDEAQNLVR LSWNHEGGDG VEFAVSYSVD GGSAQNLTTT SEMAAAATGV EPGRTYTFSV
VARSGDASSP PASVSLQIGG APEDEQPEEP AENEQEPDEN EQEPDENEQE PDENEQGDGG
NNGNPGNQNP GQGQGNGSGN QGNPNNGQGG GQGNQGGGQQ QTPGGPGGQT SPGDGSGDQG
GDGTGEETQN P
//
