ID A0A377QXH3_9NEIS Unreviewed; 696 AA.
AC A0A377QXH3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:STQ99903.1};
GN Name=penA_1 {ECO:0000313|EMBL:STQ99903.1};
GN ORFNames=NCTC13336_00090 {ECO:0000313|EMBL:STQ99903.1};
OS Kingella potus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=265175 {ECO:0000313|EMBL:STQ99903.1, ECO:0000313|Proteomes:UP000254293};
RN [1] {ECO:0000313|EMBL:STQ99903.1, ECO:0000313|Proteomes:UP000254293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13336 {ECO:0000313|EMBL:STQ99903.1,
RC ECO:0000313|Proteomes:UP000254293};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; UGJJ01000001; STQ99903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377QXH3; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000254293; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000254293};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..244
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 276..618
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 673..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 76680 MW; 10484FDA656DE84D CRC64;
MKKYRPYPAS RSDNASIQRD FRIRLFAAFV FIVALFSILA ARFAYLQIHK HSEFTAQAAS
NRISLIPTPP IRGEITDING VVLAHNYPAY SLEIIPGRIE GKLEDTVAEL QKLADITETD
LKRFKKFRAE YRSYEKVPLK LKLTPDEAAL IAARLYRLPG VEINARTFRE YPYGEQTAHF
LGYIGRISDK DQARLSEEKL TSLYRGSTHI GKSGLESYYE RQLLGTPGYR EVEKDAYGNI
IRTIKTVPPQ NGQTLKLAMD IRLQQYAMRL MKGKRGAMVA IDPQTGGVLA FVSNPSFDPN
MFIDGIDSES WKALNENWQK PMINRVTQGL YPPGSTFKPF MGMTLLESGK IGPYTVVPAP
GAWSIPGSKH MFRDSVRSGH GSANLMKAIQ VSSDTFFYRL GFETGIEKAL PYLSQFGLGQ
QTGIDLPHEY RGVLPSPEWK EKRFAKLPAA RRKWNIAEMV PISIGQGYNA YTPLQMAHAT
AILANNGTVY RPHLVKELID HNKRQITLID PKPVRTLPFK QANFNYIKAA MAKVLQPGGT
ARKVGVGLKY SMGGKTGTAQ VVQIAQGKSY NAAALAVQHR DHAWFIAFAP LDKPKIAIAV
ILENGGWGAN AAPLARALSD YYLLTLKAGS DREIPVDNSG KTTVANPLLA GGAVQRPSEN
PVTRAFRTPY PAAASSAAPV SDGLPASAAT PPESAP
//
