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Database: UniProt
Entry: A0A0Q9SML9_9MICO
LinkDB: A0A0Q9SML9_9MICO
Original site: A0A0Q9SML9_9MICO 
ID   A0A0Q9SML9_9MICO        Unreviewed;       485 AA.
AC   A0A0Q9SML9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:KRF28797.1};
GN   ORFNames=ASG91_03865 {ECO:0000313|EMBL:KRF28797.1};
OS   Phycicoccus sp. Soil802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF28797.1, ECO:0000313|Proteomes:UP000050906};
RN   [1] {ECO:0000313|EMBL:KRF28797.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF28797.1,
RC   ECO:0000313|Proteomes:UP000050906};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF28797.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF28797.1,
RC   ECO:0000313|Proteomes:UP000050906};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRF28797.1}.
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DR   EMBL; LMSS01000002; KRF28797.1; -; Genomic_DNA.
DR   RefSeq; WP_056921330.1; NZ_LMSS01000002.1.
DR   AlphaFoldDB; A0A0Q9SML9; -.
DR   Proteomes; UP000050906; Unassembled WGS sequence.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; 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; 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; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:KRF28797.1};
KW   Cell division {ECO:0000313|EMBL:KRF28797.1}.
FT   DOMAIN          156..480
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   485 AA;  51047 MW;  8476519ED5AD32C0 CRC64;
     MNSPIRRLST VVAMLFTALL ISTTYIQFVQ AKSLQDRPEN RRTLLANYAR ERGQILVGGK
     PVAKSTATDD ELKWLRTYPQ GELYSHLTGY YSFTYGAGGG IEGAENDLLS GSSDKLFYRR
     VSDILTGKEQ TGASIELTIN AKAQAAADKA LGNQRGAVVA IDPTTGEILA LVSHPAYDPA
     SLSSHDTDKV VAAWKRLNAD STQPMVDRAI AGNLYPPGST FKVVTAAAAL ESGKYTEESV
     IPGPAVLDLP QTDDDLPNDF RGSCGANNKT TLTHALEISC NTAFGWLGMQ VGADDFRAQA
     AKFGMGDRLQ IPMSVTPSSV PAELDQPQLA QSAIGQYDVR VTPLQVAMIS AAIANNGVVM
     RPHLVKKVTS SDLEVIDEPQ PEQLSQAVSA DTAAALTRMM EAVVKSGTGR AAQISGIDVA
     GKTGTAQHAK GKPPHAWFTG FAPSNDPKVA VAVVVEDGGN AGNEAAGGRV AAPIAKAVME
     AVLGR
//
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