ID A0A1M3HKG4_9SPHI Unreviewed; 741 AA.
AC A0A1M3HKG4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:OJW58835.1};
GN ORFNames=BGO55_19130 {ECO:0000313|EMBL:OJW58835.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW58835.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW58835.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW58835.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJW58835.1}.
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DR EMBL; MKTZ01000008; OJW58835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HKG4; -.
DR STRING; 1895841.BGO55_19130; -.
DR Proteomes; UP000184242; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
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 InterPro; IPR003124; WH2_dom.
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.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 668..685
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 684..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 82194 MW; 8A869ABDAE16570A CRC64;
MPVFNQSRSN IIRLIFAGMF LIIAAQLFHL QIVSKKYQQQ AQENALFRKS IYPSRGIIYD
RKGRAILNNT ILYDLMVTPG QVKNIDTAYL CQLVGIDTTE FRHRVLDARI KNGPFRPTIF
EDLLPPDMYA RLEENIWKFP GFNLQERPIR VYPFNAAAHI MGYVGEVDSS ILRRSNNFYQ
LGDYVGRSGL EQYYEKALMG QRGIEFWIKD NKNRLVNHYQ DKSLDTPAIA GKNLRTYLDI
DLQQLAERLL SGKTGAIVAL EPSTGGILAM ASGPNYDPNS LTGPDKQTNY ARLALDVSSP
MLNRAIKGQY PAGSTYKPIG ALIGLDEGVI TPASGISCLG AYLACTKPVK CDEKVPGHAA
NLRLAIAHSC NSFFCNTFRL TIDNPEYRST RKGLMKWKEY VNAFGLGHRI GVDLPSEDGG
NIPDTTAYDK DYNRNWNSCS MVTLGIGQDK MNVTPLQMAN AMCIVANKGY YYTPHFVKSI
DDAQGADSIL SKYHVKHEPV THISDDVFNV VQSGMQDVIE IGTGRPARIP GITMCGKTGT
AENKQRIDGR TLKLHNHSWF VCFAPRENPK IAVAVIVENG GYGGTWAAPI ASMIVEKYLN
DTLRNERLPE VNRIAGSNMM PKYLVRVQFR TDSMRAADYA NQTGDSARLL KYIDKANRAM
LLDTVDGSRS PLLAAIRKMP NLKPLTPRVT AAPTPAAPAQ KPDSGGHVPA LDTSAIHAVR
HKAKADTVQK PLDQKGDSTQ R
//