ID I0JKB2_HALH3 Unreviewed; 724 AA.
AC I0JKB2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpF {ECO:0000313|EMBL:CCG44581.1};
GN OrderedLocusNames=HBHAL_2228 {ECO:0000313|EMBL:CCG44581.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44581.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG44581.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE717023; CCG44581.1; -; Genomic_DNA.
DR AlphaFoldDB; I0JKB2; -.
DR STRING; 866895.HBHAL_2228; -.
DR KEGG; hhd:HBHAL_2228; -.
DR PATRIC; fig|866895.3.peg.1241; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_5_9; -.
DR Proteomes; UP000007397; Chromosome.
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 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; 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:SF36; PENICILLIN-BINDING PROTEIN 1F; 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 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:UP000007397};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 330..602
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 724 AA; 80602 MW; 55AA561582CFDF11 CRC64;
MKQYDYLKPI QRAARRVRWA GIILAILVMA GVLGYITILF GGRLVVSEED LVLDEKTFVE
TKDGEVIEEI YTKNREIIDL SDVPDHVQQA FVAIEDSRFY EHSGIDFKSI VRAVYKDIIA
MAKVEGASTI TQQLAKNISL SNDKTWMRKT KEVMAAIYLE RNFTKDEILE LYLNRIYFGE
GVYGIEAAAE HYFQSPASEL TVAEGALLAG MPKAPNSYSP FDNPEEAKER RNLVLSRMND
TGSISAADMK SYQGATLGAE EDESESETWT NSYVDLVIAE AAEKYDISRD ELKRGGYRVI
VEMDPVAQRI AAENVKNGEF VPGTNGEVQG ALTLMDHETG ALRAVVGGRD FKHGDINRVL
TAHQPASAIK PLAVYGPALM TEEYTPYTVL PDEKQEFADN YTPENYDGEY DGSVSLYQAL
SESKNVAAVW LLDQMGIDYV KGYLKELGLE TKDKGLAIAL GALSEGYTPL QMAEAYRSFA
QNGKVTDSYT ITQIKDRSGV VIHKHQSGEE TEVFSPQTAW YMTEMLQSAV SEGTASAGDY
RKALAGKTGT QQHLDGDNKD VWFAGYTPEY VGTLWMGYDQ AGENFRLEGG SSYPTRLMKD
ILSQIDEKKN LKKSFARPEG VEDLPEPIEM PDIEDASGSL SLSGLARFRG TINWTPADDD
RLVYRIYREE EGEDVKVGEV TGKGEFKVNA FGIFDQTTYY IVPFDPLTGR EGEPSNKVTL
NWDL
//
