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Database: UniProt
Entry: A0A1G1JZ29_9BACT
LinkDB: A0A1G1JZ29_9BACT
Original site: A0A1G1JZ29_9BACT 
ID   A0A1G1JZ29_9BACT        Unreviewed;       590 AA.
AC   A0A1G1JZ29;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Penicillin-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3C35_06725 {ECO:0000313|EMBL:OGW85884.1};
OS   Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_46_11.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801820 {ECO:0000313|EMBL:OGW85884.1, ECO:0000313|Proteomes:UP000176909};
RN   [1] {ECO:0000313|EMBL:OGW85884.1, ECO:0000313|Proteomes:UP000176909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGW85884.1}.
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DR   EMBL; MHFF01000046; OGW85884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1JZ29; -.
DR   STRING; 1801820.A3C35_06725; -.
DR   Proteomes; UP000176909; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   Gene3D; 1.10.150.770; -; 1.
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   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          41..186
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          232..540
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          551..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  65771 MW;  212C923EAA8ED398 CRC64;
     MNLAILATFP LIVYQLFRLT VQNHDFLRQY ARRQHNIVVE IPPERGAILD RNLKEFATNL
     KVPSIYAVPR LMLEKDRKVA AEKLSKVLGL SKPFLLERFS RDKAFVWIKR RTSVAEAEAV
     RKLKSANIGI TYEPKRFYPQ GEMLAHVIGF CNIDNIGQEG LELLYERRLA GRLGYRYTKR
     DAFGREMIAL EEKLVPPLNG ARLILTIDQY IQYVTEQALD DAFKKRHAKG ATAIVMNPKT
     GEILAMASRP TFDPNRLSES DAAHRRNRPI TDIFEPGSVF KIVTAAAALN EGKVTLQDTF
     NCENGEWQVR ASRVIHDVHP YGRLSFPEVL IKSSNIGTVK IAMRLGEEPL YRYIKQFGFG
     EKTGIDFPGE VSGILHPLNK WSKVSITSIP YGQEVAATAL QMLRAIAVIA NGGHLVKPYL
     LKEIQDANGV SLMKNEPIVS EESILKPEVV ASMNEILQRV VSEGTGTSAQ IEGIRIAGKT
     GTAQKLEPGG GYSHRHFIGS FIGYAPAEDP MLAMIVSIDD PRPYYYGGTV AAPVFKDVIE
     RSLIHLGYVP EKKPAKKTDQ KSQAISGRAS SPSLPRNPQP EFQGVSPQVR
//
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