ID A0A1H7ZRU5_9FIRM Unreviewed; 624 AA.
AC A0A1H7ZRU5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SEM60229.1};
GN ORFNames=SAMN04488698_10874 {ECO:0000313|EMBL:SEM60229.1};
OS Candidatus Frackibacter sp. WG12.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Frackibacter.
OX NCBI_TaxID=2017977 {ECO:0000313|EMBL:SEM60229.1, ECO:0000313|Proteomes:UP000199298};
RN [1] {ECO:0000313|Proteomes:UP000199298}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG12 {ECO:0000313|Proteomes:UP000199298};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FOCA01000008; SEM60229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7ZRU5; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000199298; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..222
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 282..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 261..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 69461 MW; 31B7F9EE00571AD4 CRC64;
MAVEDRFNQR VKYFGMIIIL LFIILVGRLF YLQVVLGEKY QELANGNRID IREIQAPRGK
IRAQNGKILI SNRLAYTVSI IPEKANDELN STLQKVSKIL NIDFEKMKEK VNDKLKNKAI
ILKRDISQKE LVIIEERKNE LPGVIIDKVP VRDYVYNSFG SHMLGYVGEI SASQLKRLSS
LGYEANDIVG KTGLEKEYEK YLQGIDGRKQ IEVNSLGQKI RTLGIDQPIS GNDLVLNIDF
ELQKAIEKYL KNGLKRLRKE MAQGEKNDSS SVNEGVQPPT GGAVVALNPK TGEVLALASA
PEYDLSYFSG GISISKWRAL NTNPLRPLFN RAIRSTPPSG SIFKLVTGTA AIEELGITGG
SHFYDPGYYK VGNIKFENWW TGGQGSLNFI ESIAFSNNTV FYKLGHRLYK LDKGLLQKYA
REYGLGSKTG IDLPNEESGL VPDAAWRKKT FDKRINQIWL PGYTINLSIG QGNLRTTPVQ
LASLVATVAN GGTLYSPQIV DKVIDYKGNI VKDFKSEVLN KLPVEDRTLR ILQRGMVGVT
TYGTARSAFE DFNFKVAGKT GTAQTGPGKN NHAWFSGYAP ASNPQIAIAV FLEYGDSSSN
TLPIAKKILR SYLDSKMKSE EKEE
//
