ID A0A1E8Q5V6_9MYCO Unreviewed; 818 AA.
AC A0A1E8Q5V6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:OFJ53826.1};
GN ORFNames=BEL07_10665 {ECO:0000313|EMBL:OFJ53826.1};
OS Mycobacterium grossiae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1552759 {ECO:0000313|EMBL:OFJ53826.1, ECO:0000313|Proteomes:UP000178953};
RN [1] {ECO:0000313|EMBL:OFJ53826.1, ECO:0000313|Proteomes:UP000178953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCH {ECO:0000313|EMBL:OFJ53826.1,
RC ECO:0000313|Proteomes:UP000178953};
RA Greninger A.L., Qin X., Jerome K., Vora S., Quinn K.;
RT "genome sequence of Mycobacterium sp. 739 SCH.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OFJ53826.1}.
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DR EMBL; MCHX01000020; OFJ53826.1; -; Genomic_DNA.
DR RefSeq; WP_070353058.1; NZ_MCHX01000020.1.
DR AlphaFoldDB; A0A1E8Q5V6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000178953; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 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 InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 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:UP000178953};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 699..764
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 686..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 85432 MW; FDEB97A766ADCDC3 CRC64;
MPEHPPTRPP TAVTVIKLAW CCLLASVIAA ALMFPVIGGI GLASNRASDV VANGSAQLVE
GEVPAVSTMT DAAGNPIAWL YNQRRFEVPS EQIANTMKLA IVSIEDKRFA DHNGVDWQGT
LTGLSGYLSG AADTRGGSTI EQQYIKNYQL LVVAQTEAEK RAAIETTPAR KLREIRMALT
LDKTFTKPEI LTRYLNLVSF GNGAFGVQDA AQTYFGIDAS ALNWQQAALL AGMVQSTSTL
NPYTNPDGAL ARRNLVLDTM IQNVPQEAEA LRAAKEQPLG VLPQPQELPR GCIAAGDRAF
FCDYVLEYLA RAGISKEQVA KGGYLIRTTL DPNVQAQVKS SIDGIAAPDL DGVASVMSVI
KPGKTSHPVV AMASNRTYGL NLDAGETMQP QPFSLVGDGA GSIFKVFTVA AALDMGMGIN
AQLDAPGRFE AKGLGSGGAK GCPPATWCVQ NAGNYRGQMS VTDALATSPN TAFAKLISQI
GVQRTVDMAV KLGLRSYALP GTARDYDPQS NESLADFVKR QNLGSFTLGP IEVNALELSN
VAATLGSNGV WCPPNPIDKV FDRRGQEVSV TTETCEQVVP EGLANTLANA MSKDDTGSGT
AAGSAGSVGW TLPMSGKTGT TEAHRSSGFL GFTNEFAAAN YIYDDSTSPG ELCSFPLRQC
GSGDLFGGNE PARTWFTAMK PITPDTVALP PTDPRYVDGS PGSRVPSIAG MSEGLARQRL
REAGFQVADQ STPVNSSSSA GTVVGTSPSG QTIPGAIITI QVSNGIAPPP PPPPAGIPIP
GLDPNAPPPE VGSTVVNIPG LPPITVPVLG PPPPPPPP
//
