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Database: UniProt
Entry: A0A380C7Z4_SPOPA
LinkDB: A0A380C7Z4_SPOPA
Original site: A0A380C7Z4_SPOPA 
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
//
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