ID Q2IYL4_RHOP2 Unreviewed; 584 AA.
AC Q2IYL4;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ABD06696.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABD06696.1};
GN OrderedLocusNames=RPB_1988 {ECO:0000313|EMBL:ABD06696.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD06696.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD06696.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD06696.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000250; ABD06696.1; -; Genomic_DNA.
DR RefSeq; WP_011440884.1; NC_007778.1.
DR AlphaFoldDB; Q2IYL4; -.
DR STRING; 316058.RPB_1988; -.
DR KEGG; rpb:RPB_1988; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_5; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000008809; 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 Gene3D; 3.30.450.330; -; 1.
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:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:ABD06696.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ABD06696.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..188
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 254..531
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 584 AA; 64033 MW; B1E283F90F43DFDC CRC64;
MTEPSVPLVG HHVNWRQRLV RSLIYGRDVD RDAKARARVG LAMLAFAAVY GVIAFKLTFI
AVVGDSHGTR RTASQDAIAT ARPDIVDRNG TILATDVKSP SLFGEPRRII DQDEAVELLT
ATLPDLETPE VRERLASKKG FVWLKREITP RQQADIKKLG IPGIGFLREN RRIYPTGTEV
SHLIGLVNID NQGIAGIEKW LDHNGLADLH RAGFASDRLQ KPVELAVDIR VQHALRDELL
KAKDKYKAKA ASGLVSNVNT GEIVAMVSLP DFDPNNPREA NDPDRINRLT TGVYEMGSTF
KTLTLAMALD SGKATLNSMY DARGALRYGK FAIHDTHPLG RAISLSEVFT FSSNVGAARI
ALSMGVDAHK AFLKKVGQLD RLRTELPESA SPIVPKRWGE LNTITISFGH GVAVAPLQAV
MGINAMVNGG YLIPPTFHRR SEDEAQKMAK RVVKKETSDK IRYLMRLNAE IGTARTADQI
AKGYYIGGKT GTSEKVINGR YAKKQVLNSF TAVLPADHPQ FQVLIMLDEP KPLPETHGFI
TSGWNAVPTG GKVIERIAPL LGIEPRFDLP PPDRLILASS RAAQ
//
