ID A0A2A2F5Z6_9GAMM Unreviewed; 328 AA.
AC A0A2A2F5Z6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=CK501_07865 {ECO:0000313|EMBL:PAU80358.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU80358.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU80358.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU80358.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC peptidoglycan layer to assemble the rod structure in the periplasmic
CC space. {ECO:0000256|ARBA:ARBA00002954}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 73 family. {ECO:0000256|ARBA:ARBA00007974}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC {ECO:0000256|ARBA:ARBA00006880}.
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:PAU80358.1}.
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DR EMBL; NSKD01000003; PAU80358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2F5Z6; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000218896; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.70.40; peptidoglycan hydrolase; 1.
DR InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR InterPro; IPR013377; FlaJ.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR NCBIfam; TIGR02541; flagell_FlgJ; 1.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:PAU80358.1};
KW Cilium {ECO:0000313|EMBL:PAU80358.1};
KW Flagellum {ECO:0000313|EMBL:PAU80358.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PAU80358.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000218896}.
FT DOMAIN 164..322
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 328 AA; 36284 MW; A5D33E605C1F3421 CRC64;
MIQSSAGGTS DAHVYTDMSA MSDLKRLADT DRDKALEKVA KQFESLFLQQ MMKSMRSANE
VFSEGNYLNS QETEQYQDMF DKQLTLSLTR ERSIGIADQL VRQLGGGEQG ADRPDARTSI
TEYSRDLPAP DPKLAERVDE VRQMMPEEGN AGSGSADGGG KELPEQFNGP EQFVQELSPI
ARDVSEKTGV PAQVMIAQAA LETGWGRNMI GGEQEPSRNL FGIKADERWN GDKVEITTTE
YRDGLPLKEK ADFRAYPDYA SSFEDYASFL NENPRYQKVL QQADDPQAFA QALQDAGYAT
DPGYADKIQN IMERPTLGAV IDDGTEGE
//
