ID A0A177QJ77_9BACT Unreviewed; 624 AA.
AC A0A177QJ77;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AYO43_05435 {ECO:0000313|EMBL:OAI46907.1};
OS Nitrospira sp. SCGC AG-212-E16.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1799664 {ECO:0000313|EMBL:OAI46907.1, ECO:0000313|Proteomes:UP000078320};
RN [1] {ECO:0000313|Proteomes:UP000078320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-E16 {ECO:0000313|Proteomes:UP000078320};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OAI46907.1}.
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DR EMBL; LSTC01000084; OAI46907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177QJ77; -.
DR STRING; 1799664.AYO43_05435; -.
DR Proteomes; UP000078320; Unassembled WGS sequence.
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 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000078320};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 19..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..229
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 262..594
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 624 AA; 67769 MW; B777EAB1FB1FC586 CRC64;
MATAGLHDSE LGELQRRLII LRVGLLLVVA LLGLQLWNLQ IREGPYYRDL SENNRTRSVI
MEPARGLIYD RNGVLLANNV PSFTLYVSLE DVKDRDLLID QLSSLLGLDE ALVRKKLTAR
GSKQLPRKVK DRLTLREATL IESHRLDLPG VMVQVESQRN YPGGVTASHL LGYVGEVSPE
QLEKPEFADL HQGSIVGQYG VEKFFDQLMR GQAGQKSIEV DAIGHEKRTV IVEQPHAGDD
LYLTIDVRLQ KVAENLLGEE SGAIVALDPR TGDVLAMASR PGFDPNILSR ELTPKQWADI
VQDEGRPLNN RASQGQYPPG SVFKVMMAAA ALETKTVTPS TSIFCNGGYQ FGRRVYHDWK
AGGHGSVDLR HALVHSCDVY FYTVGQRMGI ETMASFAHQF GLGEETGIEL PSERVGIVPS
EAWKRKAKNE AWLPGETISA SIGQGYVNVT PLQMATLIGT VANDGVMFRP RLVQAVMDRA
TGEVQQRSAV PKRTLKLRPG ILPMIKEALA GVVKEGTGTR AQSALVTIAG KTGTAQTLAL
RTGPEKDIPK KFRDHAWFVA FAPVDAPTIA VAVLGEHMGH GGSASAPLAK ELIETYVKLN
LSAPPGAKDG AVARVGDAGG QGTR
//