ID A0A124ICJ4_9ACTN Unreviewed; 415 AA.
AC A0A124ICJ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQJ58_12090 {ECO:0000313|EMBL:KUO12200.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO12200.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO12200.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO12200.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:KUO12200.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMXA01000009; KUO12200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124ICJ4; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053431; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13432; LDT_IgD_like_2; 1.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.60.40.3710; -; 1.
DR Gene3D; 2.60.40.3780; -; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR041280; Big_10.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR Pfam; PF17964; Big_10; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000053431};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..415
FT /note="FHA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007174235"
FT DOMAIN 68..229
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 253..385
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 27..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 43675 MW; FEC812C2B6300517 CRC64;
MTDSRRRRGL MTASALLGGV LMLTACSSGD SSASDGKDSS SQAKADEAAA KKSSEAQIKI
TPADGSNNAS INNSAAVTVS KGTLTAVTMT TAEGTAVEGT LSADKTSWKP NAQLERSTTY
KVAASAKDSK GLAAHENASF TTVSPDNSFI ANFTPEDGST VGVGMPVSIN FNKEITNKAD
VQKGITVTSS SGQEVVCHWF STVRMDCRPE DYWKENSTVT LKLALDGVEG AKGVVGVQQK
TVTFKIGRNQ VTTVDAQTKQ MKVTQDGKVV KTIPISAGSP DNKTYEGQMV ISEKFKETRM
NGATVGFTDD DGKGEYDIKD VPHAMRLTTS GTFVHGNYWG AKSIFGAVNT SHGCVGLSDT
KGANDPSTPA AWFYTNSIIG DVVVVKNTGD KTVAPDNGLN GWNMDWAQWK AGSAV
//
