ID F4KJR8_PORAD Unreviewed; 618 AA.
AC F4KJR8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:AEE12645.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:AEE12645.1};
GN OrderedLocusNames=Poras_0695 {ECO:0000313|EMBL:AEE12645.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12645.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) 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; CP002689; AEE12645.1; -; Genomic_DNA.
DR RefSeq; WP_004331478.1; NC_015501.1.
DR AlphaFoldDB; F4KJR8; -.
DR STRING; 879243.Poras_0695; -.
DR KEGG; pah:Poras_0695; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_10; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000006545; Chromosome.
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 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: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:AEE12645.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW Transferase {ECO:0000313|EMBL:AEE12645.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..223
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 261..579
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 618 AA; 68783 MW; 30EF1F62224DF3E1 CRC64;
MERSRHRLRI AVLPMIAISI VVLYVIRLGY LQLVSSEYKE RAMRNALYEE VIFPDRGVIY
DRKGTLLVYN EPAYDLLVTT KELADTLDMP LLSSLLHTSE LELKDRMTAL RDRSINPGYS
PFTPQLFWSQ LTSEEAGFIQ EQLFRLPGFT LRPRAVRRSD QPNAALLLGY LGESSPEELK
ADSTLALGQY VGKSGVERTY DSILRGRNGV NLLLRDARGR IQGSYNDGAD DIEAIPGEDL
TLSIDIGLQS LGEKLLQGKR GAIVMIEPKS GEVLCLVSSP SYDVRLLQGK SLGKAHQQLV
LQEGKPLFNR AIMGTYPPGS TFKPAMGALM LQEHLVTPST LLSCAHGYPR MRGRPACHGH
ASPLNLRSAL TTSCNAYFCW GLHFLLDDRT RYPSVQDALN KWRDYMVDFG FGYKLGVDLA
GENRGFIPNS SVYDRVYRRW NSSTIISLSI GQGEVLLTPL QMANLAATIA NRGYYYKPHV
VRKIEHSPLD SIYRTPHHTI VSPGYWEEIA QGMHGAVLAG TCRRANFAPG EINVCGKTGT
AENRFGKDHS AFIGFAPLED PKVAISVYVE NGGFGAIYGV PIGRVMMEYY LRDGELSGTS
QAIVEQISRQ KIFYTHDT
//
