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Database: UniProt
Entry: A0A1F8NMD5_9CHLR
LinkDB: A0A1F8NMD5_9CHLR
Original site: A0A1F8NMD5_9CHLR 
ID   A0A1F8NMD5_9CHLR        Unreviewed;       706 AA.
AC   A0A1F8NMD5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2Y53_02880 {ECO:0000313|EMBL:OGO12020.1};
OS   Chloroflexi bacterium RBG_16_47_49.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797639 {ECO:0000313|EMBL:OGO12020.1, ECO:0000313|Proteomes:UP000179729};
RN   [1] {ECO:0000313|EMBL:OGO12020.1, ECO:0000313|Proteomes:UP000179729}
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:OGO12020.1}.
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DR   EMBL; MGNG01000087; OGO12020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8NMD5; -.
DR   Proteomes; UP000179729; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; 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   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   4: Predicted;
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..250
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          299..692
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   706 AA;  77343 MW;  C551167AF1FC21C2 CRC64;
     MKSSPALKNM VETWRIIFLG SLLVVIFFIY VARLYDLQVV QYSDWLAKSN ENRTHEINLP
     ASRGTIYDRK GYIVARNIPS YNVVITPADL PDDTGEIQTI YREISNLTGI PVNRGEVSTS
     DPYVPCISDH GITEIVTYGE TTAPYEPVKI TCDINQQIAL AIQENASTWP GVGIEVVPVR
     DYPTGSLTAS IVGFLGPIPA IDEDYYRTMG FVPNRDKVGY AGVELYFQNL LAGVNGHRVV
     EWDIAGQILD DLVPPVSSTP GSSIVLTIDT RLQQAVQSIL ADEINDWNRA LGEERMTSGA
     VIAINPRTGE ILSLVNYPTY ENNRLARVIP AYYYQQLISD KRNPLLNLAV GAELPAGSVF
     KLVTATGGLN EGIVTPEEII KTPGKITVTE RFYANDPGRP RDFVDWIYRT RPEGFGQLDF
     VHAVANSSNV YFYKVGGGYQ DEVDPGLGIC RLGTYARALG YGTLPEGYAG LPAGYSTPEI
     ELPDVASGLI PDPTWKRINQ GESWSTGDSY IVSVGQGYAL ATPLQVLLSA ATVANNGKLM
     APTILYEILD SEGNIIQPFM PRLRWDLTVD PVIQSYEDNT IRGCQLTGKM KTVEPWVFDQ
     IRTGMRLAVL EGTLKSIFTN VNIAAAGKTG TAEYCDEFAK AKNLCEPGNW PSHAWTVAFA
     PYEDPEIAVV AFVYNGGEGA SVAGPIVRRV LEAYFELKSA DSTVIP
//
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