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Database: UniProt
Entry: N0E479_9MICO
LinkDB: N0E479_9MICO
Original site: N0E479_9MICO 
ID   N0E479_9MICO            Unreviewed;       634 AA.
AC   N0E479;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Penicillin-binding protein transpeptidase {ECO:0000313|EMBL:CCH70625.1};
GN   ORFNames=BN10_620006 {ECO:0000313|EMBL:CCH70625.1};
OS   Phycicoccus elongatus Lp2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH70625.1, ECO:0000313|Proteomes:UP000013167};
RN   [1] {ECO:0000313|EMBL:CCH70625.1, ECO:0000313|Proteomes:UP000013167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lp2 {ECO:0000313|EMBL:CCH70625.1,
RC   ECO:0000313|Proteomes:UP000013167};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:CCH70625.1}.
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DR   EMBL; CAIZ01000133; CCH70625.1; -; Genomic_DNA.
DR   RefSeq; WP_010850468.1; NZ_HF570956.1.
DR   AlphaFoldDB; N0E479; -.
DR   STRING; 1193181.BN10_620006; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_025328_0_0_11; -.
DR   OrthoDB; 5241017at2; -.
DR   Proteomes; UP000013167; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013167}.
FT   DOMAIN          151..310
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          349..624
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   634 AA;  64261 MW;  23AEA89D858808EA CRC64;
     MRSRPALLAS LIAVALVAVV GTVGWRWYST ERDREAGSKS ALAAYVKGWN TKTMTGVSFD
     TAGVAEDFTK TVAGMATAPV SANAESLARD GQTATARLTV DWTLPGDRHW KYALPVSLAE
     RGGHWVVLAP EGGSRWSPDL PEGASLSIKT VQAKRGDLLD RGGAALMPMS SVYPVQIDPV
     RATPESAAGL EGVTGEPAGS LVAKLAAAKA SGSAAPIPVI TYRQADFDAR KAALDALVGV
     IYPRSEAPLA PTRTFGQPLL GTYGAVTADL VTASKGRYAA GDRAGLSGLQ LQYDQTLAGK
     PGLQVVASTG KVLFEEAAVD GEDVGTTLSV AVQDAAEKAL VAGGSVPSAI VAIDVATGEV
     VAAANSPGDG MNRALTGHYA PGSGFKVAST MALLEKGLVT PETVVDCPPT ITVDGKSFRN
     FEGGEATGVT FARDFALSCN TAFIGLSGTL APGDLAASGK ALGIGAGWTD RIGVTGTFEG
     SIPETTPGTD LAASVIGQGR IEVSPLSMAV AAGSMARGAF LAPTLVKVGA GATTPAPAAL
     PQPALDQTRA LMRSVVTEGS GTALQGAPGG DVFGKTGTAE YGTEVPPKTR AWFVGYQGDL
     AFAVLVEDGR SGGSVAAPIA RSFLDLYRAA PTAE
//
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