ID A4SFF8_CHLPM Unreviewed; 635 AA.
AC A4SFF8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ABP37217.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABP37217.1};
GN OrderedLocusNames=Cvib_1205 {ECO:0000313|EMBL:ABP37217.1};
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318 {ECO:0000313|EMBL:ABP37217.1};
RN [1] {ECO:0000313|EMBL:ABP37217.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 {ECO:0000313|EMBL:ABP37217.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP000607; ABP37217.1; -; Genomic_DNA.
DR AlphaFoldDB; A4SFF8; -.
DR STRING; 290318.Cvib_1205; -.
DR KEGG; pvi:Cvib_1205; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_10; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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 InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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:ABP37217.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ABP37217.1};
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 54..217
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..578
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 635 AA; 69802 MW; 0AE6CAEEC1432CF8 CRC64;
MMDTYQRSTS TAILFVVAIF SLLLGRLFWL QVLDFQQLGS VGASASIRRI WELPPRGRMM
DRNGKIMIDN RPLYSAKLIP SEFDSSRTAA LAWLIKMPES DIAEHIAEGT RYNRFSALTL
KRDLSTEDAA RLSENIWKLP GVIIAAENKR KYADSLYGAH MFGYLRSISP AQFKELKEEG
YARDDKIGFS GLERQYESHL RGIKGTRFIM VTPLGRNAGR YDEGRSDIPA IRGNDLSLSI
DMELQKLAGK LLAETGKSGA VVAIDPRTGG ILALQSAPDF NLEVFNGATD PAGWENIRSN
PQKPLFNRTV QAVYPPGSIY KMVLATAALE EKTIDPDKKV LDNGVFRFGN RQYLSHRGEG
HGMVDMREAI TVSSNVYFYS LIFDVGFTAW TNYGALFGFG KRTGIDLPGE RSGLLPSSDY
YNRRYGKGRW TKGNLVSLAI GQGELGTTPI QLATYAAAIA NRGTLHQPHI VEGYRDTRTG
TYVPFRYRQH RLPLKPETLE LIRGSMADVV QTGTGRLAQV PGIAVCGKTG TAQNPHGKDH
AWFIAYAPAD NPEIALTVLV ENAGYGGSVS APIAGKLIRQ YLKHMIPVPS VPVGASTPDT
FIEANPLTPA IVPALKDSSI SLTVPSPPEK ETNDQ
//
