ID D5V3R9_ARCNC Unreviewed; 478 AA.
AC D5V3R9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:ADG92747.1};
GN OrderedLocusNames=Arnit_1085 {ECO:0000313|EMBL:ADG92747.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG92747.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG92747.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
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DR EMBL; CP001999; ADG92747.1; -; Genomic_DNA.
DR RefSeq; WP_013134892.1; NC_014166.1.
DR AlphaFoldDB; D5V3R9; -.
DR STRING; 572480.Arnit_1085; -.
DR KEGG; ant:Arnit_1085; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_035297_0_0_7; -.
DR OrthoDB; 9801978at2; -.
DR Proteomes; UP000000939; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ADG92747.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..335
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 478 AA; 55343 MW; F59B082463B956C2 CRC64;
MEYFNIFTHL VLVMSLGWYL ITNLQWYSYK LERVVFKHHK LHWHIIYFVT PFVMYYLLPS
LYFLVYFYAL YLPLLILWNM KLDKPLVLTS RVQRFLAILL FVTFSISLLC FVSENCKSAG
IFIPLFIAYL VSFSLERIFF ISFKHRAKKR LQSIKDLKII AITASYGKTS IKNYLYQILK
SKFNAYKTPR SVNTLAGLVL DVNRDLPENT QIYIAEAGAR MQGDIEEISN FLHQDYAILG
QVGEQHIEYF KTLDNIIHTK MEILKSPKMI KAFVHESVPI LDYEKIEKFP NDLNITKSNL
DGIWFDVNID EKQEHFYAPI LGSFNAVNLT ACILMAKELG MSIDQIKIAL DKIKPVEHRL
QKIEAGGKVI IDDSFNGNFE GMLEAVNLCS EYKGRKVIIT PGLVESTDET NILLAKEINK
HFDFVILTGS LNTHLFSDNI DKNKQFILKD KSKMEETLIE KTRAGDLILF ANDAPNFI
//
