ID A0A1H3W541_9FIRM Unreviewed; 949 AA.
AC A0A1H3W541;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SDZ82197.1};
GN ORFNames=SAMN02910384_00225 {ECO:0000313|EMBL:SDZ82197.1};
OS Pseudobutyrivibrio sp. ACV-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520801 {ECO:0000313|EMBL:SDZ82197.1, ECO:0000313|Proteomes:UP000199179};
RN [1] {ECO:0000313|Proteomes:UP000199179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
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; FNQZ01000001; SDZ82197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3W541; -.
DR STRING; 1520801.SAMN02910384_00225; -.
DR Proteomes; UP000199179; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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); 2.
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: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 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..321
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 605..920
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 949 AA; 105881 MW; 64665DBEBA962614 CRC64;
MEIIKDFLKN AFSSRIRVVI VTMVFFAMVL IMRLFYLQII NGSEYQDHYN LKLEKTETIP
ATRGNIYDRN GNLLAYNELV YAVTIQDTGT YSSSRERSQS LNSEIAQIIT KLESNGDSID
NNFPITIDSA GAYQFLYSGN SLQRFRADVF GRNSIDDLDY NEKLGLDEAT ATAEQIVNYL
EGPKVYNISD EYDKELKYKI LVVRYSMGQN SYQKYISTVI ASDISEKSVA YVEENVNELT
GVAIEQKSLR RYTDSEYFAH IIGYTGQIST SEYKELSKKD DTVETTDVVG KSGIEQYMND
YLSGTKGYET LYVDSVGNTI AKGDSKVATS GNDVYLSIDM ELQKATYILL EQEIAGILYS
KIANIKQFNS SENGSASDVV VPIYDVYYSL IGNGIIDINA FSNSNATSTE KAVLAAYEKR
QKQVLATLKS QLTSDNEVIY SDLPKEYQAY STYIVTKLKS LGIFDSSAID TSSEVQTTWT
SEQMAVNKYL IYAIEQNWID ITKYEIEAKY ADTEELYNDL IDYILDYLSN DKAFKNLIYK
YLLLDDGITG TQLCMILYDQ GVLKEDEETY QMLASGRLSS YEFMLSKIKN LEITPGQLAL
DPCSGSSVIL DTNTGEVLAM VTYPGYDNNR LANSVDADYY AYLTNSAANP LYNYATQQRT
APGSTFKIVS STAGLAENVI TTETQITDLG QYFKVSNHPK CWIYPSNHGS INVSEAIRDS
CNYFFYEVGW RLAGGDGAYD DIKGIEKIQK YASLYGLDET TGVEVEENSP HIATEYPVMA
AIGQSDNNFT TVGLARYATA IASKGTVYNL TLLDSVRDSD GKVLKSYGPS VRNQMDVLQD
YQWDAIHHGM RMVVESLSSY NNFSVPVAGK TGTAQQVRSR PNHALFIGFA PYDNPEVAIA
TRIAYGYTSH NAAAVSKDIL SYYFGVSSTE EILNGEASTV SDSVDEFTD
//
