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Database: UniProt
Entry: A0A0F0H3Z6_9ACTN
LinkDB: A0A0F0H3Z6_9ACTN
Original site: A0A0F0H3Z6_9ACTN 
ID   A0A0F0H3Z6_9ACTN        Unreviewed;       723 AA.
AC   A0A0F0H3Z6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KJK50235.1};
GN   ORFNames=UK14_13790 {ECO:0000313|EMBL:KJK50235.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK50235.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK50235.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK50235.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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}.
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:KJK50235.1}.
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DR   EMBL; JYJI01000101; KJK50235.1; -; Genomic_DNA.
DR   RefSeq; WP_030027167.1; NZ_JYJI01000101.1.
DR   AlphaFoldDB; A0A0F0H3Z6; -.
DR   PATRIC; fig|1609137.3.peg.2929; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000033569; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Reference proteome {ECO:0000313|Proteomes:UP000033569};
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..658
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          672..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..713
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  78722 MW;  904437E8BC3491E9 CRC64;
     MTNVPETGRT SRVQIRLVIM QVLVFSMLIT LGGRLWFLQI RNGAEYYHEA KSNHVQRVVQ
     PAVRGSILDA RGVPLADNET RLVVSASRTA LMKMKDKGRG VLTRLADVLD MTPKQVMDKV
     RLCDSQTPKP CWNGSPYQPI PVTLEATTQQ ALQLRERPEE FPGITAEPTA VRRYPAPGGA
     RTAQVLGYLS PVTDDEIQKA KDTDSPHLRS DQVGRSGLER TYDRQLRGKA QVTSYEVDNL
     GRVMGQTRSD PGIAGSTLVT SIDARVQAVA EYELQQAMKV VRNETDNITG RKYEADSGAV
     VVMEAKTGRI VAMASQPDYD PNAWVGGISG ADYAKLTSKN SNYPLLNRAI QGMAPAGSIF
     KVVSASAAVR AGYKFNDRYN CSSSYSLGGR SFANFESKGH GPITLGEALK FSCNTVFYAL
     GHKEWQRDGG LSPKKDAHDW FYRTAREFGL GSETGIDLPN EVKGRIPDRQ WKQSFWAANK
     NSWCKQGKRG GTYVEQIAYE SCLEGNQLKA YDSINFAIGQ GDVLVTPIQM ATAYSAISNG
     GTLYNPTVGK AVISPDGKHV EILKPQSHGR LPVNAQTVAD LDRGLRMVVE PGGTAAWRFG
     GWPQDKIPMH AKTGTAQVYG KQTTSWLATY TKDFTIVMTI SQGGTGSGAS GPAVRNLYNA
     LYGLTMDGKP NQKGALLPAP ETKLPKINPD GSIESPEIRP YVPPSPEDLQ APALAGPPPT
     RHD
//
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