ID A0A380C7Z4_SPOPA Unreviewed; 670 AA.
AC A0A380C7Z4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SUJ14182.1};
GN Name=penA_2 {ECO:0000313|EMBL:SUJ14182.1};
GN ORFNames=NCTC4822_02393 {ECO:0000313|EMBL:SUJ14182.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ14182.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ14182.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; UGYZ01000002; SUJ14182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380C7Z4; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000254519; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000254519};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..670
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039167021"
FT DOMAIN 27..149
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 157..316
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 357..667
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 670 AA; 74434 MW; ED282D2E2D4D5CC3 CRC64;
MRKLRYGILF LGLILTLAAC SKEEDTPVDR LSAYVDLWND AKFTEMYDDY ITESSKDVFG
KEQFIERAEK LYADLGISSI EVIFDKPEEE KTYKKEEDVE FPVQIKLETI AGEIDFKKNV
PLTYKEQGET KNWFIEWDPS FILPDLSMHD KVRISTIQSK RGEIYDRHNK ALAINGSGVE
IGIVPEKFNT ETDAEKLATL LGTTANFINE QLNQSWVQPD LFVPIKKLSF TQEDIYNEAL
QIAGVTSMKA EMREYPYAES LAHLIGYIGQ INAEELEKLN DKGYKESDLV GKRGLEQLLE
ERLRGEDGIK IYIEKTEQNA EKIMIAETPA IDGENITLTI DAEFQKAVFA EMNGEPGTAA
IVDPKTGETL VLASSPAFDP NELSLGISST RYAELTDDPA EPLLNRFAAT YAPGSSIKPI
TAAIGLSTGT LKPDEGHTIE GKKWRKDGSW GNFQVTRVYT APNPVDLKKA LVYSDNIYFA
KEALEMGSEQ FVEGLQQFGF GEEIPFKYGL RTSQISNDGK ITSEGQLADT SFGQGQMLMN
ILHLASTYGA IVNEGQMTKP VLFADEKKSE VWKEELLSAE HAAILQEDLR AVVSDGFAEA
ANISSPKISG KTGTTELKSS LEEAGKENGF FVAYPTDDPT YIIAMMIEGV ENKGGSGYVA
EKVANVMKTR
//