ID A0A0S1SD48_9FLAO Unreviewed; 622 AA.
AC A0A0S1SD48;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:ALM08036.1};
GN ORFNames=SB49_09660 {ECO:0000313|EMBL:ALM08036.1};
OS Sediminicola sp. YIK13.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM08036.1, ECO:0000313|Proteomes:UP000063759};
RN [1] {ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA Kwon Y.M., Kim S.-J.;
RT "Genome sequence of Sediminicola sp. YIK13.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM08036.1, ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|EMBL:ALM08036.1,
RC ECO:0000313|Proteomes:UP000063759};
RX PubMed=26823585;
RA Kwon Y.M., Kim S.J.;
RT "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT Bacterium Sediminicola sp. YIK13.";
RL Genome Announc. 4:e01635-15(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP010535; ALM08036.1; -; Genomic_DNA.
DR RefSeq; WP_062056051.1; NZ_CP010535.1.
DR AlphaFoldDB; A0A0S1SD48; -.
DR STRING; 1453352.SB49_09660; -.
DR KEGG; syi:SB49_09660; -.
DR PATRIC; fig|1453352.4.peg.2011; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000063759; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000063759}.
FT DOMAIN 46..207
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 247..577
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 622 AA; 70351 MW; E005F248E93CBA44 CRC64;
MNKFLLSAFI IIIGITFIGR LSYLQVFNNV GEKVSEDVAV KAIYDYPERG YIYDRNGELL
VANQPAYDVM VIPKDVKPLD TLEFCILLGL EKEQFIKNLN KAKIYSPRLP SVLVHQLSKE
DYARLQEKMR KYDGFYIQKR SLRYYATNSG ANVLGYISEV NERDLANNPY YKQGELLGKT
GIEKEYENIL RGKKGVKYIQ KDRFNRDIGP YKNGALDTLP EQGKEIHVTL DKKLQEYGEL
LMQGKHGGIV AIEPNSGEIL ALISGPTYDP ALLVGRERSK NYTKLYYDSI SKPTYDRSLL
AETSPGSPFK ILNALVALQE GAITPDTKIM CYHGFYVGST KRGCHCGGGM RDMTSGIYNS
CNAYFAGTFR KIYEQFPTTD AGMDVWEKHM KSFGLGDFLG YDLPTGKRGR IPSKEYYDKW
YGDNRWSSSY IISNSIGQGE VSATPIQLAN MTAAIANKGF YYTPHVLKKI DHEDISIPEF
IKAKHTTIDK KYFDPVINGM AMVYKQGTAS RLQIPDIEIA GKTGTVENFT RIDGVKTQLT
DHSVFIAFAP VENPKIAIAV YIEHGYFGSR YAGHIASLLI EKYLKGEITR TDLEKRMLEK
NLEAEYAKPH SGQPFIINER VW
//
