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Database: UniProt
Entry: F5X5E5_STRPX
LinkDB: F5X5E5_STRPX
Original site: F5X5E5_STRPX 
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}.
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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
//
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