ID B9L2H2_THERP Unreviewed; 725 AA.
AC B9L2H2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:ACM06279.1};
GN OrderedLocusNames=trd_1373 {ECO:0000313|EMBL:ACM06279.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM06279.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM06279.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP001275; ACM06279.1; -; Genomic_DNA.
DR RefSeq; WP_015922323.1; NC_011959.1.
DR AlphaFoldDB; B9L2H2; -.
DR STRING; 309801.trd_1373; -.
DR KEGG; tro:trd_1373; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_0; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000000447; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 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; 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 69..181
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 188..351
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 387..715
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 725 AA; 79040 MW; A6CF956AF4387A44 CRC64;
MPRATVRSSR RRSASGSLVA GLLIFAIVTG GIVAVALQFG DRQDTTTIGV ADQSSASATL
TRELAAPRTA REAAERFVRA WEERDYRAMY ALLSSAARQQ IDEAQFIRRY EAISAEMGER
SLQVTLGEAL PGTMRFPIHV VRETTRVGRL EEDNAIPIVR EGDAFRIDWT PSLIVADLGD
GRVEWIPTVP QRGRLLDVKG RPLAQLGLVN KVGVVPGQIR DEHLLLERLS TLLNVPSETI
RQRYAGGQPD WFMPVATLPD PIDPGLLEQL AGIPGVVVRQ WPERVYPLGP AAAHVTGYLS
EVSAEELERR AADGYEPGDR IGRAGIEAWA EDFLRGRRGG RLVIVGPDGR ERRFLAEIPA
QPAADVLTTI DTDLQEAAYR ALGDRVGSVV AIDPRSGAIR ALVSNPSFDP NRFILGLRTD
EWQALNDEQR RPLIDRATQV GYPTGSTFKV VTMAAGLAYL GLRAESRFDC PPTFSLPGSS
VVWRDWNPRG QGQLTLHDAL VQSCNTVFFQ IGAQLDERDP NLLPQMARAF GFGSETGLTE
LPETAGLVPD PSWKRRERGD YWARGDAVNL SIGQGFFLAT PLQLADAYAA LANGGTLWQP
FLVERVVAID GSERFHAEPK ARGALPLTPE QIDTIRAALR DVVARPNGTA WSAFQGFTVS
VAGKTGTAES GQETPHAWFV AIAPAENPEL VLVVMVEHGG EGSRVAAPIA RQILETAQQA
GYFQR
//
