ID F5X5E5_STRPX Unreviewed; 708 AA.
AC F5X5E5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Penicillin-binding protein 2B {ECO:0000313|EMBL:BAK29635.1};
DE EC=2.3.2.- {ECO:0000313|EMBL:BAK29635.1};
GN Name=pbp2B {ECO:0000313|EMBL:BAK29635.1};
GN OrderedLocusNames=SGPB_0523 {ECO:0000313|EMBL:BAK29635.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK29635.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK29635.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012054; BAK29635.1; -; Genomic_DNA.
DR RefSeq; WP_013851591.1; NC_015600.1.
DR AlphaFoldDB; F5X5E5; -.
DR STRING; 981540.SGPB_0523; -.
DR KEGG; stb:SGPB_0523; -.
DR HOGENOM; CLU_009289_7_0_9; -.
DR Proteomes; UP000007946; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase 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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR047982; PBP2B.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; NF038278; strep_PBP2B; 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 Acyltransferase {ECO:0000313|EMBL:BAK29635.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW Transferase {ECO:0000313|EMBL:BAK29635.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..319
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 368..698
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 708 AA; 76680 MW; C11F4387B6731CCE CRC64;
MSFKKRLSKL KFAKKTTEKK VRKFKIDKKP TSMTKRIYLI FSVIVVLFSI IILRLAQMQI
LNKSFYDEKL NSSTTYTVTT SNPRGEIYDA AGNLLVSNTV KQVVAFTRSN TITAEEMKEL
AAKLSTLVTF TETNVTTRQK KDYYLADSDT YAAVVKSLPD DEKYDSYGNN LTESEIYANA
INAVTDDEIN YSEDELKLVY IFSQMNAAST FSTVNLTTGD LTEEQIAYIT ANQSKLSGIS
IATDWDRETP TSSLASIIGT VSSKHSGLPA EEADDYLAKG YSLNDRVGTS YLEKEYEEYL
QGTHTVREIT TDKNGNVVSD EVTSEGKAGQ NLKLTVNSDF QAGVESILNQ YYSADIADGY
ATYSEGAYAV ALNPQTGAIL AMAGLSHETG SSTTTLDALG TINDIFVPGS VVKAATLTAG
WESDAISGNQ VIADQSINIA GSSAITSWFT GSGSTNITAV QALEYSSNTY MVQVALKMMG
QEYYSGMSLA TTGMKEAMEE LRAAYAEYGM GTSTGIDLPE NTTGYISDDY SAGNVLTEAF
GQYDSYTPMQ LAQYAATVAN GGKRIAPHLV DSIYDNDGTA GIGTLGKTIE TNVLNQINIS
DDDMDLLQQG FYQVVNSSSA YATGTYMKSS TVTIAGKTGT AETYAVDANG NAVTTVNLSV
LAYDYSTSDD SHIAVAVIIP HLTSSDNHTN QYIARDIINL YMSTYVNQ
//