ID   A0A1S2HI89_9MICO        Unreviewed;       574 AA.
AC   A0A1S2HI89;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Penicillin-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BIU96_17460 {ECO:0000313|EMBL:OII11181.1};
OS   Curtobacterium sp. MCBA15_008.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII11181.1, ECO:0000313|Proteomes:UP000180168};
RN   [1] {ECO:0000313|EMBL:OII11181.1, ECO:0000313|Proteomes:UP000180168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII11181.1,
RC   ECO:0000313|Proteomes:UP000180168};
RA   Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT   "Evidence for ecological flexibility in the cosmopolitan genus
RT   Curtobacterium.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:OII11181.1}.
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DR   EMBL; MJGN01000025; OII11181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S2HI89; -.
DR   STRING; 1898736.BIU96_17460; -.
DR   Proteomes; UP000180168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   Gene3D; 3.30.450.330; -; 1.
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   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          40..199
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          244..551
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   574 AA;  60579 MW;  826F0A931A9AAE43 CRC64;
     MIAVIALVAV FVIRLVDIQV VQAADLNEQS KQKRSIPVTI YGTRGSIVDR SGTELADSVT
     RYNITTAPRL VKKFEGKLGG TRVKEVSVDT ALSALAEASG GDVATMKKNI AANPKSDFAY
     LVKGLDVKHY EAVRALSIPW LYPEQQSARS YPTAATTGNL TGFMGTDGAQ AGLELAYDKC
     LAGSNGSETY ERGEDGVQLP GSTVTTKKAK DGGTLETTID SDLQYMAGQT IASAAKTLQA
     ESATATVTSV KTGELLAVAD YPTVDPNDVD ATTDKGAFGS RALTASYEPG STIKAAIAAA
     LIDQGKSSPT DGITVPYTRS FPWGGSIKDA EFHPTEHLTL AGVLQNSSNV GITELGERLT
     KQQRFDYMKK FGLFQPESAI DYPGQPSMDY GTSPNWDDQT NINSMFGQGI STTAVQIASV
     FQTIANQGVR IPLHFVKGCE TADGKTIDAP DVQPTRVVSA SAATQVTDML QNVVKGGTLS
     GMAPISGYNI AAKTGTAEVA EGSKGYGGQR IISVAGMAPA EDPQYVVTVT FTKPQTTKFS
     SGAAPAFRTL MSQVLEKYRV APSTSQAKLY PSTW
//