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Entry: G2NHE7_STREK
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Original site: G2NHE7_STREK 
ID   G2NHE7_STREK            Unreviewed;       723 AA.
AC   G2NHE7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AEN09931.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:AEN09931.1};
GN   ORFNames=SACTE_2029 {ECO:0000313|EMBL:AEN09931.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09931.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN09931.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN09931.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(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; CP002993; AEN09931.1; -; Genomic_DNA.
DR   RefSeq; WP_014045917.1; NC_015953.1.
DR   AlphaFoldDB; G2NHE7; -.
DR   STRING; 862751.SACTE_2029; -.
DR   KEGG; ssx:SACTE_2029; -.
DR   PATRIC; fig|862751.12.peg.2112; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_11; -.
DR   OMA; SCDTYYY; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:AEN09931.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   Transferase {ECO:0000313|EMBL:AEN09931.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..246
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          298..657
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          679..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  78603 MW;  CE348CBEB2FDB452 CRC64;
     MSNIPETGRT QRVQIRLVVI QILVFSLLLT LGGRLWYLQI RNGQEYTDEA KNNHVQQVVQ
     PAVRGSILDA RGVPLADNET RLVVSASRTE LMKMKDDGVG VLTRLAEVLD MKPKDVQDKV
     RLCDAKTPQP CWNGSPYQPI PVTDEATTQQ ALQIRERAED FPGITAEPTA VRRYAAPGKA
     NTAQVLGYLS PVTDEELTKA QDTDSPYLRS DQVGRSGLER TYDKELRGKA GVTRYEVDNL
     GRVIGEAQND EAQPGASVVT SIDARVQAVA EYELDQAMKA ARKEMDRNTN EFYKADSGAV
     VVMEAKTGRV VSMASLPTYD PNSWVGGISA KDYAELTGKK SNFPLLNRAI QGTAAPGSIF
     KVISSTAAVN AGYPFDGNYP CPSSYSIGNQ TFKNFESQGY GNITIGRALE VSCDTVYYGI
     AHKEWQKDGG NKPKKNANDW FYKTAHQFGL GKETGIDLPN EVAGRVPDRQ WKQDFYDANR
     ESWCKQGKKD GTYVEQLAYE GCAEGYKMRA GDSVNYSIGQ GDTLVTPIQM ATIYAAISNG
     GTLYDPTVGK AIVSGDGRTV QEIEPQAHGK LPFTGDTRDK IDQALAGVAT QGSAAWRFGG
     WPQDKIPMHA KTGTAEVYGK QTTSWFATYT KDYSIVMTIS QGGTGSGASG PAVRNIYNAI
     YGLDGEGKQD LKKALLPQPQ KALPKITPDG SIVSPKIKPY TPEPPADEGT QALALAVAPG
     RRD
//
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