ID A0A139XCU2_9CYAN Unreviewed; 604 AA.
AC A0A139XCU2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KYC42514.1};
GN ORFNames=WA1_21380 {ECO:0000313|EMBL:KYC42514.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC42514.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC42514.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC42514.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC42514.1}.
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DR EMBL; ANNX02000020; KYC42514.1; -; Genomic_DNA.
DR RefSeq; WP_017748918.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139XCU2; -.
DR STRING; 128403.WA1_21380; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..238
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 271..588
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 604 AA; 66528 MW; 9AF3EC41CF68873C CRC64;
MALLQSPQPL TKKRETRTVG RGSQPLFLII FTLLLTAGIG ARLAYLQIVE GPKLRERAES
NRIRMISKQP ERGNIFDRNG KLLATTRYPR SVYLWPMSHT KPSWSVVGPR LSKIIDMPED
EIIKKLEEAG PNMTLVRIAR DLNEAEITAL KEYANELQTV EIHTEAVRFY PHGQALAHVL
GYTRELTSKQ LREKKKDGYR LGDVIGQMGV EKAYEKTLRG EWGGQQVEVD GKGRPIRVLG
EKQAKAGNDI HLTLDLNLQK AAEKALNGRD GSIVALDPNK GAVLAMVSHP TFDPNIFSKQ
KVSKKDWQTV QGENHPLLNR AVSSAYPPAS TFKIVTTTAG LESGKFSPNT VLQTYGSLTV
GGVTFGEWNH AGFGPLGFTG AMAWSSDTFF YQIGRGVGGP GLIEWTRKYG FGKKTGVEFV
SEETKGNVPD EAWKQRVWKM PWTVGDSINM SIGQGALQTT PLQVAVMFAV PANGGYRVKP
HLLKDNEELK NWRESLNMKP STVKVLREGL RKVVSEGTGK ALNVQTIPPS SGKSGTAEAW
KRRVKANHAW FGAYGPYDKP EIVVLAFAEH SGGGGGSVAA PMVLQVMEEY FRHKSPSKSQ
KAGN
//
