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Database: UniProt
Entry: A0A177QJ77_9BACT
LinkDB: A0A177QJ77_9BACT
Original site: A0A177QJ77_9BACT 
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
//
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