ID A0A1F8TCM6_9CHLR Unreviewed; 724 AA.
AC A0A1F8TCM6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Z49_06565 {ECO:0000313|EMBL:OGO69904.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_56_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797670 {ECO:0000313|EMBL:OGO69904.1, ECO:0000313|Proteomes:UP000177731};
RN [1] {ECO:0000313|EMBL:OGO69904.1, ECO:0000313|Proteomes:UP000177731}
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:OGO69904.1}.
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DR EMBL; MGOL01000131; OGO69904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8TCM6; -.
DR Proteomes; UP000177731; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
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; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 42..154
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 164..332
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 365..692
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 724 AA; 78467 MW; D6A3870F26C1ADAE CRC64;
MLALLLVGCS QPGPSVEASP PPPPTPTLPL PGVNTTQAPD VESAARAYLE AWKADDYTKM
YAMLTSVSQD ALTEEEFAQI YSRVATEAAL SSLDPQILSS LTQTRSAQVS YRVNLHSALV
GDIVRDTLMN LSLEDGKWRV QWDETLILPE LGGGNTLRMD RLIPSRANIY DRDGQALVAQ
ADATALGVFP DQIDPDQENT LLSELWRLTG LYPDNIHARY ENFPPGAGWY LPLLAVPADL
VQQREGVLSG LAGLVLSPFR SRFYFDGGIA PHVIGYVSAI PAEEVGEYQR QGYLQDERVG
QAGLEKWGEA YLSGKRGGAL YVVDPNGATV TKLAESPAEP AQAIFTTLDK ELQLGAQQAI
EGFKGAVVIL ERDTGRVIAM ASSPGFDPNL FEPANLNSGY EIGELFDQNT IPLLNRATQG
QYPLGSVFKI ITMAAALESG IYTPETVYDC QHTFTELQGV TLYDWTFEKE LPASGPLTLP
EGLMRSCNPY FYHIGNDLYN QGLTNAVSDM ARGFGLGQAT GIDQVAEVEG QVPDPASNLD
ATNLSTGQGA LQVTPLQVVD FIAAIGNGGI LYRPQVVERI APPDGDPAVI FKPEVRGKLP
ISAQTLHTIQ EAMISVIENR RGTAHRVFAN FPIDIAGKTG TAQDPPRDPH AWFAGYTFDE
RTDKPDVAAV VVLENAGEGS EVAAPIFKGL MQLYFFGKRD SFPWETLPGV WKTPTPEVTE
TPQP
//