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Database: UniProt
Entry: A0A239JPJ9_9ACTN
LinkDB: A0A239JPJ9_9ACTN
Original site: A0A239JPJ9_9ACTN 
ID   A0A239JPJ9_9ACTN        Unreviewed;       636 AA.
AC   A0A239JPJ9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:SNT07811.1};
GN   ORFNames=SAMN05421812_10363 {ECO:0000313|EMBL:SNT07811.1};
OS   Asanoa hainanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Asanoa.
OX   NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT07811.1, ECO:0000313|Proteomes:UP000198362};
RN   [1] {ECO:0000313|EMBL:SNT07811.1, ECO:0000313|Proteomes:UP000198362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT07811.1,
RC   ECO:0000313|Proteomes:UP000198362};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; FZPH01000003; SNT07811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239JPJ9; -.
DR   OrthoDB; 5241017at2; -.
DR   Proteomes; UP000198362; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:SNT07811.1};
KW   Cell division {ECO:0000313|EMBL:SNT07811.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198362};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..636
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039156734"
FT   DOMAIN          28..139
FT                   /note="NTF2-like N-terminal transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF05223"
FT   DOMAIN          148..314
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          362..630
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   636 AA;  65436 MW;  0CF13B5DAFC8D7FA CRC64;
     MTRRPAALLA GLALVAAGLA GCSSDPGPDD AVDSFLSAWK SGDLSQIAFV EPTGSKVAAT
     EVQAALKELS GELTPPVVRR EGEPKEVEGS ATAAVDLDWT LPGGTHWTYP STVRLIKGGD
     DVWSVIWEPA IVNAKLKSGD QLALRRQRPE RAGILDGAGK PIVEPRDVVV VGVEPAGVDD
     PAGIARALDS AFKSVRPALP KIDVSDLPAK INSAEDPEQF LEVVTLRRDA YLQIRSKIQP
     LEGTRFREEK RDLAPTRAFA RALLGSADPA LKEDIDKRPD EVAEGDLVGH GGLQGALDKQ
     LRGTPGVSVV IANKGPDGEV TDGEELWRSE AKAGTPVKTT LDVSVQNAAD TALSGLRQRS
     ALVAVRVSDG AVLAAANGPD GGSGENLAFT AQVPPGSTFK MVSGYGLLSS GKVTATTSVD
     CPKTFTVDGR SFKNSENFAL GKVPFQVDFA KSCNTAFASL APSLGDDGLA LAGRALGLEA
     KWDLGVDAFS GKVSTGGSAA ERAAAAFGQG TTLVSPLSMA SATASVAKGS AVTPKILADK
     PAAGDGAALK AEALGPLKSM MRQVVTSGTA TALKDVPGGA VSGKTGTAEF DDNPAHTHAW
     FVGWQGDIAF AVFVENGGGS GTTAVPAAER FIRALH
//
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