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Database: UniProt
Entry: A0A2S1YX17_9ACTN
LinkDB: A0A2S1YX17_9ACTN
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ID   A0A2S1YX17_9ACTN        Unreviewed;       724 AA.
AC   A0A2S1YX17;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AWK08664.1};
GN   Name=mrdA {ECO:0000313|EMBL:AWK08664.1};
GN   ORFNames=DDQ41_06690 {ECO:0000313|EMBL:AWK08664.1}, SSP531S_14600
GN   {ECO:0000313|EMBL:GBQ00052.1};
OS   Streptomyces spongiicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK08664.1, ECO:0000313|Proteomes:UP000245051};
RN   [1] {ECO:0000313|EMBL:AWK08664.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HNM0071 {ECO:0000313|EMBL:AWK08664.1};
RA   Zhou S., Huang X.;
RT   "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT   HNM0071, the producer of staurosporine.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GBQ00052.1, ECO:0000313|Proteomes:UP000265354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=531S {ECO:0000313|EMBL:GBQ00052.1,
RC   ECO:0000313|Proteomes:UP000265354};
RA   Dohra H., Kodani S.;
RT   "Whole Genome Shotgun Sequence of Streptomyces spongiicola strain 531S.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CP029254; AWK08664.1; -; Genomic_DNA.
DR   EMBL; BGZL01000003; GBQ00052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1YX17; -.
DR   KEGG; sspo:DDQ41_06690; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000245051; Chromosome.
DR   Proteomes; UP000265354; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..245
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          678..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  78883 MW;  999E51D72BAF7920 CRC64;
     MSNIPETGRT PRVQIRLIVI QVLVFSLFAT LGGRLWYLQI RNGDEYTNEA KGNHVQQVVQ
     PAVRGSILDA RGVPLADNET RLVVSASRTD LMRMKDDGKG VLTRLAEVLG MKPKDVMDKV
     RLCDAKTPQP CWNGSPYQPI PVTDEATTQQ ALQIRERAED FPGITAEPMA VRRYAAPGEA
     NTAQVLGYLS PVTDEEIEKA KDTDSPFLRS DQVGRSGLER TYDKDLRGKA GVTRYEVDKL
     GRVIGLAQAD KAEPGANVVT SIDARVQAVA EWELDNAMKE ARKVFDDNTN TNYKADSGAV
     VVMEARTGRV VAMASLPTYD PNAWVGGISA KDYARLTGKK SNFPLLNRAI QGQAAPGSIF
     KVIPTTAAVN AGYDFNGRYP CPSSYSIGNQ VFKNFESQGH GSITLGQALE VSCDTVYYAL
     AHQQWKKDGG LKPKDDPADW FYKTAHQFGL GAETGIDLPN EVTGRVPDRR WKQKFWEANK
     DYWCKIGKKG GDYIQQLSYE NCLEGNLMRA GDSVNYSIGQ GDTLVTPIQM ATIYAAISNG
     GTMWNPTVGK AVISADGRSI REIEPESHGK LPMDARTRKL MNEALAGVAT RGTAAWRFGG
     WPQDKIPMHA KTGTAEVHGK QTTSWFATYT KDYSIVMTIS QGGTGSGASG PAVRNIYNAL
     YGLDMEGNQD LGKALLPQPQ KTLPKVQPDG SIDAPKITPY APAQPEPEED TSLAGPPPAT
     GRRD
//
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