ID Q47M14_THEFY Unreviewed; 643 AA.
AC Q47M14;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Similar to Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:AAZ56508.1};
GN OrderedLocusNames=Tfu_2475 {ECO:0000313|EMBL:AAZ56508.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56508.1};
RN [1] {ECO:0000313|EMBL:AAZ56508.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ56508.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP000088; AAZ56508.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47M14; -.
DR STRING; 269800.Tfu_2475; -.
DR KEGG; tfu:Tfu_2475; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_025328_0_0_11; -.
DR OrthoDB; 5241017at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:AAZ56508.1};
KW Cell division {ECO:0000313|EMBL:AAZ56508.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..643
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004233689"
FT DOMAIN 32..140
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 149..312
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 349..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 643 AA; 67256 MW; 50260C17B8598EA7 CRC64;
MPPRNSLRRF LAATTGALLV TATAACAAEP SPEVAVRSFL LNWQEGDYEA AAQVTNGDVA
EVAEALRQAH NQLDLAALRL SLRPIEMDGD TATAGFGAEA DLGIGDPVWR YTGTIPLTRT
DSGWVIDWSP AVIHPELGEG ERLAVTYDVP DRGQIYDRNG EPLVEETEVT AFGVRPAAMA
DMTEGINSLA ELLDEDPEPL LNRVRSAPPE EFQPLVLKRT QDVSSSLLAK ATAIPGVEVE
EGTMPLLPIR AAGVVGEVAG TAEHKVANRV SGPYQAGDTV GLNGLQSSFQ QQLAGTATTR
VVTLSSSGEE TGVLETWTGE ESGSLTTTLD HAVQEAAETS LATINGTAYL VAVDARSGEI
LAAAGQPDEP SNDGALTRQY YPGETFTIVS AAALLSGGKA TLDTTMACEQ QAEVGSRTFT
NPNGGSLLGT PDLRTNFAYS CTTAFVGLSS SLSAADLAES AERFGIGQPW QLPVPAFSGE
FTVQGGQEQV AAATVGADGI TVSPLGMALV AAAVAGGQWH APRLIDGVEP EVDSIPVDPA
VLEPLRELMR APVEQGSASV LNIDYVNPVH GQTGMVTQEI DGEEKTIQWF VGYRGHVAFA
VVVEAAPSHT YQFAVNSALS FLQLLPASYV SAAEADSQLE GSA
//
