ID A0A075K7X1_9FIRM Unreviewed; 619 AA.
AC A0A075K7X1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AIF49732.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:AIF49732.1};
GN ORFNames=UFO1_0171 {ECO:0000313|EMBL:AIF49732.1};
OS Pelosinus sp. UFO1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF49732.1, ECO:0000313|Proteomes:UP000027983};
RN [1] {ECO:0000313|EMBL:AIF49732.1, ECO:0000313|Proteomes:UP000027983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF49732.1};
RX PubMed=25189589;
RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT Single-Molecule Real-Time DNA Sequencing Technology.";
RL Genome Announc. 2:e00881-14(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP008852; AIF49732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075K7X1; -.
DR STRING; 484770.UFO1_0171; -.
DR KEGG; puf:UFO1_0171; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_9; -.
DR Proteomes; UP000027983; 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 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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:AIF49732.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027983};
KW Transferase {ECO:0000313|EMBL:AIF49732.1};
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 53..220
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..589
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 619 AA; 67408 MW; 2C17059E10FFC049 CRC64;
MTKGSTSQRL NVLTFIIVSI FIALLSRLVW LQALHGEEFK QKAENNRIRL LPITAPRGTF
YDRNGLPLVN NRPGFSISLV PIKGPIPKEI IVRLAEILGM NPDDIQKKMS QQGNPLLPTR
IKSDVGPEII TKIEERREDL PGVVIEVQAV RSYIYNELGA HTFGYVGEIS DSQLAKGKVS
GYKSGDMLGK TGLEQVWDKE LRGVDGGAQV EVNVSGKPVQ MLGKKQPIAG NDLILTINAK
IQRAAEKAMD ERLKYLQDKL GNPEAKAAAA VVMNPQTGEI LAIVSRPTFD PNKFNGGISA
KDWKEINDNP NNPMQNRTIG ASYPPGSAFK IVTGTAALET GKVTPEEKIF DSGRHRLAPA
KGNAHNAALG WIDFRVALAK SDNVYFYELG NRLGIDTLEQ WARKFGLGAV TGINLPDEDD
GLVANQRYKK KVYDEDWVIS ETFDAAIGQG FNLATPLQMA VVTSIAANGG HRYRPYLVSK
MVSPSGQVVQ TFEPEELGTV PMSPSTLNAI RTGLRDVVTP SGTAGYIFEG FPVPIAGKTS
TAENPHGDDH GWFVAYGPYD NPTIAIAVIV EQGGYGSDSA APIARKIMEA AFDLPPSRDA
ADIYAEEWQT KQNNKITSQ
//
