ID A0A1Q2H2J1_9GAMM Unreviewed; 787 AA.
AC A0A1Q2H2J1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=B0W48_18385 {ECO:0000313|EMBL:AQQ01575.1};
OS Pseudoalteromonas aliena.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ01575.1, ECO:0000313|Proteomes:UP000188243};
RN [1] {ECO:0000313|EMBL:AQQ01575.1, ECO:0000313|Proteomes:UP000188243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH1 {ECO:0000313|EMBL:AQQ01575.1,
RC ECO:0000313|Proteomes:UP000188243};
RA Kim E., Heo E., Kim H., Kim D.;
RT "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT strain EH1 isolated from Arctic seawater.";
RL Submitted (FEB-2017) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP019628; AQQ01575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2H2J1; -.
DR STRING; 247523.B0W48_18385; -.
DR KEGG; paln:B0W48_18385; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000188243; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..217
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 311..535
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 697..778
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 787 AA; 88554 MW; 133FF85B4B7375CC CRC64;
MLLPLNKKYS VRIKLVLLTT ALLAVLWYVF VPKPDITQST TYSTAFYDSS GKLLRLNLAT
DDRYRLWMPI ERIPLSVQQA TLLYEDQYFY QHIGIDFIAL TKAFYTSYIK RSRRVGASTI
TMQVARLRFG MNTHVVLGKI EQIFRALQIE RHYNKKQILE AYFNLAPYGS NIEGIGAASL
IYFNKPAFEL NLPESLLLSL VPQNPSKRNP IKQSAKAILL DARQTLFSRW LEAYPSDKNW
SATMQLPISV HSSSELPFEA PHFINNLQSK FPHLESAEYK TTINLSLQKL LERHGKSYIK
RREREGITNT SAILLNYQTM EIVAELGSVD FFNNTISGQV NGTRAKRSPG STLKPFIYAL
AIDEGLIHPL SLVKDAPKRF GGYTPENYDQ QFLGPISATD SLVLSRNVPA VNLMYRLKKV
GLYDLLVAAD IKKLQPKEFY GLALALGGNE VTMLELVKLY AVLANLGMYQ NEIILQQEPE
RDLKNNTKKR LLSPEAAYLT LQMLSKNNAV DEISFQQQSR KTYPVYWKTG TSFAFRDAWS
VGIVGPYVLA TWVGNFSGEG HPSFIGRQAA APLFFEIIRS LESYGLIKGD IKRGGLNIEK
VDICSTTGDL PNVHCPKTQK GLFIPGKSPI KISDVHREIF IDKASGSRAC RFDESTTTKA
IYEFWPSDLI RLFKQAGIVK RQPPAYLASC AINDTSTLGS APTITSPSNL ISYTVRASKL
TQESLPFTAT TDTDSSALYW FVNNSFVGKV ERDTAFFWQP KIGIFEVKVV DNLGRSSSTT
LRVKLVQ
//
